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Protein folding

Index Protein folding

Protein folding is the physical process by which a protein chain acquires its native 3-dimensional structure, a conformation that is usually biologically functional, in an expeditious and reproducible manner. [1]

149 relations: Ab initio, Alan Fersht, Allergy, Alpha helix, Alzheimer's disease, Amino acid, Amphiphile, Amyloid, Anfinsen's dogma, Antibody, Anton (computer), Application-specific integrated circuit, Aqueous solution, Backbone chain, Bengt Nölting, Beta sheet, Bovine spongiform encephalopathy, C-terminus, Central processing unit, Chaperone (protein), Chemical kinetics, Chevron plot, Chris Dobson, Chronic obstructive pulmonary disease, Circular dichroism, Circular polarization, Coarse-grained modeling, Comparison of software for molecular mechanics modeling, Conformational entropy, Covalent bond, Creutzfeldt–Jakob disease, Cysteine, Cystic fibrosis, D. E. Shaw Research, Denaturation (biochemistry), Denaturation midpoint, Disease, Distributed computing, Disulfide, Downhill folding, Dual-polarization interferometry, Energy landscape, Enthalpy, Entropy, Enzyme, Equilibrium unfolding, European Medicines Agency, Fast parallel proteolysis, Fibril, Fluorescence spectroscopy, ..., Folding (chemistry), Folding funnel, Folding@home, Foldit, Fourier transform, Fourier-transform infrared spectroscopy, Gibbs free energy, Graphics processing unit, Harry B. Gray, Heat shock protein, Huntington's disease, Hydrogen bond, Hydrogen–deuterium exchange, Hydrophobic collapse, Hydrophobic effect, Hyperthermophile, Immune system, In silico, In vitro, In vivo, Intramolecular force, Intrinsically disordered proteins, José Onuchic, Lattice protein, Levinthal's paradox, Linus Pauling, Lipid bilayer, List of protein structure prediction software, London dispersion force, Lysosomal storage disease, Macromolecule, Martin Gruebele, Messenger RNA, Molecular dynamics, Multiple isomorphous replacement, N-terminus, Nanosecond, Native state, Neurodegeneration, Neutron scattering, Nuclear magnetic resonance spectroscopy, Optical tweezers, Parkinson's disease, Peptide, Peptide bond, Peter Guy Wolynes, PH, Pharmacological chaperone, Phi value analysis, Physical change, Picosecond, Potential energy of protein, Precipitation (chemistry), Prion, Protein, Protein biosynthesis, Protein design, Protein domain, Protein dynamics, Protein folding, Protein misfolding cyclic amplification, Protein primary structure, Protein quaternary structure, Protein secondary structure, Protein structure, Protein structure prediction, Protein tertiary structure, Proteolysis, Proteopathy, Quantum yield, Ramachandran plot, Random coil, Reaction intermediate, Ribosome, Rosetta@home, Salt (chemistry), Self-assembly, Sheena Radford, Solubility, Solution, Solvent, Spontaneous process, Stanford University, Statistical potential, Stopped-flow, Tafamidis, Temperature, Temperature jump, Thermodynamic free energy, Thermostability, Three-dimensional space, Time-resolved mass spectrometry, Translation (biology), Umbrella sampling, Van der Waals force, Vibrational circular dichroism, Von Willebrand factor, Water, X-ray crystallography. Expand index (99 more) »

Ab initio

Ab initio is a Latin term meaning "from the beginning" and is derived from the Latin ab ("from") + initio, ablative singular of initium ("beginning").

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Alan Fersht

Sir Alan Roy Fersht, FRS, FMedSci (born 21 April 1943) is a British chemist at the Laboratory of Molecular Biology and an Emeritus Professor in the Department of Chemistry at the University of Cambridge.

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Allergy

Allergies, also known as allergic diseases, are a number of conditions caused by hypersensitivity of the immune system to typically harmless substances in the environment.

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Alpha helix

The alpha helix (α-helix) is a common motif in the secondary structure of proteins and is a righthand-spiral conformation (i.e. helix) in which every backbone N−H group donates a hydrogen bond to the backbone C.

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Alzheimer's disease

Alzheimer's disease (AD), also referred to simply as Alzheimer's, is a chronic neurodegenerative disease that usually starts slowly and worsens over time.

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Amino acid

Amino acids are organic compounds containing amine (-NH2) and carboxyl (-COOH) functional groups, along with a side chain (R group) specific to each amino acid.

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Amphiphile

An amphiphile (from the Greek αμφις, amphis: both and φιλíα, philia: love, friendship) is a chemical compound possessing both hydrophilic (water-loving, polar) and lipophilic (fat-loving) properties.

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Amyloid

Amyloids are aggregates of proteins that become folded into a shape that allows many copies of that protein to stick together forming fibrils.

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Anfinsen's dogma

Anfinsen's dogma (also known as the thermodynamic hypothesis) is a postulate in molecular biology that states that, at least for a small globular protein in its standard physiological environment, the native structure is determined only by the protein's amino acid sequence.

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Antibody

An antibody (Ab), also known as an immunoglobulin (Ig), is a large, Y-shaped protein produced mainly by plasma cells that is used by the immune system to neutralize pathogens such as pathogenic bacteria and viruses.

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Anton (computer)

Anton is a massively parallel supercomputer designed and built by D. E. Shaw Research in New York.

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Application-specific integrated circuit

An Application-Specific Integrated Circuit (ASIC), is an integrated circuit (IC) customized for a particular use, rather than intended for general-purpose use.

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Aqueous solution

An aqueous solution is a solution in which the solvent is water.

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Backbone chain

In polymer science, the backbone chain of a polymer is the longest series of covalently bonded atoms that together create the continuous chain of the molecule.

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Bengt Nölting

Bengt Nölting (1 May 1962 - 16 September 2009) was a German physicist and biophysicist who pioneered various methods in biophysics and engineering.

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Beta sheet

The β-sheet (also β-pleated sheet) is a common motif of regular secondary structure in proteins.

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Bovine spongiform encephalopathy

Bovine spongiform encephalopathy (BSE), commonly known as mad cow disease, is a transmissible spongiform encephalopathy and fatal neurodegenerative disease in cattle that may be passed to humans who have eaten infected flesh.

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C-terminus

The C-terminus (also known as the carboxyl-terminus, carboxy-terminus, C-terminal tail, C-terminal end, or COOH-terminus) is the end of an amino acid chain (protein or polypeptide), terminated by a free carboxyl group (-COOH).

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Central processing unit

A central processing unit (CPU) is the electronic circuitry within a computer that carries out the instructions of a computer program by performing the basic arithmetic, logical, control and input/output (I/O) operations specified by the instructions.

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Chaperone (protein)

In molecular biology, molecular chaperones are proteins that assist the covalent folding or unfolding and the assembly or disassembly of other macromolecular structures.

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Chemical kinetics

Chemical kinetics, also known as reaction kinetics, is the study of rates of chemical processes.

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Chevron plot

A chevron plot is a way of representing protein folding kinetic data in the presence of varying concentrations of denaturant that disrupts the protein's native tertiary structure.

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Chris Dobson

Sir Christopher Martin Dobson, FRS, FMedSci (born 8 October 1949) is a British chemist, who is the John Humphrey Plummer Professor of Chemical and Structural Biology in the Department of Chemistry at the University of Cambridge, and Master of St John's College, Cambridge.

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Chronic obstructive pulmonary disease

Chronic obstructive pulmonary disease (COPD) is a type of obstructive lung disease characterized by long-term breathing problems and poor airflow.

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Circular dichroism

Circular dichroism (CD) is dichroism involving circularly polarized light, i.e., the differential absorption of left- and right-handed light.

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Circular polarization

In electrodynamics, circular polarization of an electromagnetic wave is a polarization state in which, at each point, the electric field of the wave has a constant magnitude but its direction rotates with time at a steady rate in a plane perpendicular to the direction of the wave.

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Coarse-grained modeling

Coarse-grained modeling, coarse-grained models, aim at simulating the behaviour of complex systems using their coarse-grained (simplified) representation.

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Comparison of software for molecular mechanics modeling

This is a list of computer programs that are predominantly used for molecular mechanics calculations.

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Conformational entropy

Conformational entropy is the entropy associated with the number of conformations of a molecule.

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Covalent bond

A covalent bond, also called a molecular bond, is a chemical bond that involves the sharing of electron pairs between atoms.

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Creutzfeldt–Jakob disease

Creutzfeldt–Jakob disease (CJD) is a universally fatal brain disorder.

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Cysteine

Cysteine (symbol Cys or C) is a semi-essential proteinogenic amino acid with the formula HO2CCH(NH2)CH2SH.

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Cystic fibrosis

Cystic fibrosis (CF) is a genetic disorder that affects mostly the lungs, but also the pancreas, liver, kidneys, and intestine.

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D. E. Shaw Research

D.

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Denaturation (biochemistry)

Denaturation is a process in which proteins or nucleic acids lose the quaternary structure, tertiary structure, and secondary structure which is present in their native state, by application of some external stress or compound such as a strong acid or base, a concentrated inorganic salt, an organic solvent (e.g., alcohol or chloroform), radiation or heat.

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Denaturation midpoint

Assuming two-state protein folding, denaturation midpoint is defined as that temperature (Tm) or denaturant concentration (Cm) at which both the folded and unfolded states are equally populated at equilibrium.

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Disease

A disease is any condition which results in the disorder of a structure or function in an organism that is not due to any external injury.

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Distributed computing

Distributed computing is a field of computer science that studies distributed systems.

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Disulfide

In chemistry, a disulfide refers to a functional group with the structure R−S−S−R′.

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Downhill folding

Downhill folding is a process in which a protein folds without encountering any significant macroscopic free energy barrier.

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Dual-polarization interferometry

Dual-polarization interferometry (DPI) is an analytical technique that probes molecular layers adsorbed to the surface of a waveguide using the evanescent wave of a laser beam.

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Energy landscape

In physics, chemistry, and biochemistry, an energy landscape is a mapping of all possible conformations of a molecular entity, or the spatial positions of interacting molecules in a system, or parameters and their corresponding energy levels, typically Gibbs free energy.

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Enthalpy

Enthalpy is a property of a thermodynamic system.

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Entropy

In statistical mechanics, entropy is an extensive property of a thermodynamic system.

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Enzyme

Enzymes are macromolecular biological catalysts.

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Equilibrium unfolding

In biochemistry, equilibrium unfolding is the process of unfolding a protein or RNA molecule by gradually changing its environment, such as by changing the temperature or pressure, adding chemical denaturants, or applying force as with an atomic force microscope tip.

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European Medicines Agency

The European Medicines Agency (EMA) is a European Union agency for the evaluation of medicinal products.

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Fast parallel proteolysis

Fast parallel proteolysis (FASTpp) is a method to determine the thermostability of proteins by measuring which fraction of protein resists rapid proteolytic digestion.

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Fibril

Fibrils (from the Latin fibra) are structural biological materials found in nearly all living organisms.

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Fluorescence spectroscopy

Fluorescence spectroscopy (also known as fluorometry or spectrofluorometry) is a type of electromagnetic spectroscopy that analyzes fluorescence from a sample.

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Folding (chemistry)

In chemistry, folding is the process by which a molecule assumes its shape or conformation.

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Folding funnel

The folding funnel hypothesis is a specific version of the energy landscape theory of protein folding, which assumes that a protein's native state corresponds to its free energy minimum under the solution conditions usually encountered in cells.

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Folding@home

Folding@home (FAH or F@h) is a distributed computing project for disease research that simulates protein folding, computational drug design, and other types of molecular dynamics.

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Foldit

Foldit is an online puzzle video game about protein folding.

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Fourier transform

The Fourier transform (FT) decomposes a function of time (a signal) into the frequencies that make it up, in a way similar to how a musical chord can be expressed as the frequencies (or pitches) of its constituent notes.

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Fourier-transform infrared spectroscopy

Fourier-transform infrared spectroscopy (FTIR) is a technique used to obtain an infrared spectrum of absorption or emission of a solid, liquid or gas.

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Gibbs free energy

In thermodynamics, the Gibbs free energy (IUPAC recommended name: Gibbs energy or Gibbs function; also known as free enthalpy to distinguish it from Helmholtz free energy) is a thermodynamic potential that can be used to calculate the maximum of reversible work that may be performed by a thermodynamic system at a constant temperature and pressure (isothermal, isobaric).

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Graphics processing unit

A graphics processing unit (GPU) is a specialized electronic circuit designed to rapidly manipulate and alter memory to accelerate the creation of images in a frame buffer intended for output to a display device.

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Harry B. Gray

Harry Barkus Gray (born 14 November 1935 in Woodburn, Kentucky, U.S.A.) is the Arnold O. Beckman Professor of Chemistry at California Institute of Technology.

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Heat shock protein

Heat shock proteins (HSP) are a family of proteins that are produced by cells in response to exposure to stressful conditions.

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Huntington's disease

Huntington's disease (HD), also known as Huntington's chorea, is an inherited disorder that results in death of brain cells.

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Hydrogen bond

A hydrogen bond is a partially electrostatic attraction between a hydrogen (H) which is bound to a more electronegative atom such as nitrogen (N), oxygen (O), or fluorine (F), and another adjacent atom bearing a lone pair of electrons.

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Hydrogen–deuterium exchange

Hydrogen–deuterium exchange (also called H–D or H/D exchange) is a chemical reaction in which a covalently bonded hydrogen atom is replaced by a deuterium atom, or vice versa.

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Hydrophobic collapse

Hydrophobic collapse is a proposed process for the production of the 3-D conformation adopted by polypeptides in polar solvents.

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Hydrophobic effect

The hydrophobic effect is the observed tendency of nonpolar substances to aggregate in an aqueous solution and exclude water molecules.

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Hyperthermophile

A hyperthermophile is an organism that thrives in extremely hot environments—from 60 °C (140 °F) upwards.

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Immune system

The immune system is a host defense system comprising many biological structures and processes within an organism that protects against disease.

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In silico

In silico (literally cod Latin for "in silicon", alluding to the mass use of silicon for semiconductor computer chips) is an expression used to mean "performed on computer or via computer simulation." The phrase was coined in 1989 as an allusion to the Latin phrases in vivo, in vitro, and in situ, which are commonly used in biology (see also systems biology) and refer to experiments done in living organisms, outside living organisms, and where they are found in nature, respectively.

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In vitro

In vitro (meaning: in the glass) studies are performed with microorganisms, cells, or biological molecules outside their normal biological context.

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In vivo

Studies that are in vivo (Latin for "within the living"; often not italicized in English) are those in which the effects of various biological entities are tested on whole, living organisms or cells, usually animals, including humans, and plants, as opposed to a tissue extract or dead organism.

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Intramolecular force

An intramolecular force is any force that binds together the atoms making up a molecule or compound, not to be confused with intermolecular forces, which are the forces present between molecules.

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Intrinsically disordered proteins

An intrinsically disordered protein (IDP) is a protein that lacks a fixed or ordered three-dimensional structure.

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José Onuchic

José N. Onuchic is a Brazilian and American physicist, the Harry C & Olga K Wiess Professor of Physics at Rice University.

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Lattice protein

Lattice proteins are highly simplified computer models of proteins which are used to investigate protein folding.

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Levinthal's paradox

Levinthal's paradox is a thought experiment, also constituting a self-reference in the theory of protein folding.

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Linus Pauling

Linus Carl Pauling (February 28, 1901 – August 19, 1994) was an American chemist, biochemist, peace activist, author, educator, and husband of American human rights activist Ava Helen Pauling.

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Lipid bilayer

The lipid bilayer (or phospholipid bilayer) is a thin polar membrane made of two layers of lipid molecules.

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List of protein structure prediction software

This list of protein structure prediction software summarizes commonly used software tools in protein structure prediction, including homology modeling, protein threading, ab initio methods, secondary structure prediction, and transmembrane helix and signal peptide prediction.

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London dispersion force

London dispersion forces (LDF, also known as dispersion forces, London forces, instantaneous dipole–induced dipole forces, or loosely van der Waals forces) are a type of force acting between atoms and molecules.

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Lysosomal storage disease

Lysosomal storage diseases (LSDs) are a group of about 50 rare inherited metabolic disorders that result from defects in lysosomal function.

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Macromolecule

A macromolecule is a very large molecule, such as protein, commonly created by the polymerization of smaller subunits (monomers).

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Martin Gruebele

Martin Gruebele (born January 10, 1964 in Stuttgart, Germany) is a German-born American physical chemist http://www.chemistry.illinois.edu/faculty/Martin_Gruebele.html Gruebele's chemistry page and biophysicist who is currently James R. Eiszner Professor of Chemistry, Professor of Physics, Professor of Biophysics and Computational Biology at the University of Illinois at Urbana-Champaign where he is the principal investigator of the.The James R. Eiszner Endowed Chair was previously held by Peter Guy Wolynes.

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Messenger RNA

Messenger RNA (mRNA) is a large family of RNA molecules that convey genetic information from DNA to the ribosome, where they specify the amino acid sequence of the protein products of gene expression.

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Molecular dynamics

Molecular dynamics (MD) is a computer simulation method for studying the physical movements of atoms and molecules.

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Multiple isomorphous replacement

Multiple isomorphous replacement (MIR) is historically the most common approach to solving the phase problem in X-ray crystallography studies of proteins.

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N-terminus

The N-terminus (also known as the amino-terminus, NH2-terminus, N-terminal end or amine-terminus) is the start of a protein or polypeptide referring to the free amine group (-NH2) located at the end of a polypeptide.

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Nanosecond

A nanosecond (ns) is an SI unit of time equal to one thousand-millionth of a second (or one billionth of a second), that is, 1/1,000,000,000 of a second, or 10 seconds.

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Native state

In biochemistry, the native state of a protein or nucleic acid is its properly folded and/or assembled form, which is operative and functional.

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Neurodegeneration

Neurodegeneration is the progressive loss of structure or function of neurons, including death of neurons.

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Neutron scattering

Neutron scattering, the irregular dispersal of free neutrons by matter, can refer to either the naturally occurring physical process itself or to the man-made experimental techniques that use the natural process for investigating materials.

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Nuclear magnetic resonance spectroscopy

Nuclear magnetic resonance spectroscopy, most commonly known as NMR spectroscopy or magnetic resonance spectroscopy (MRS), is a spectroscopic technique to observe local magnetic fields around atomic nuclei.

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Optical tweezers

Optical tweezers (originally called "single-beam gradient force trap") are scientific instruments that use a highly focused laser beam to provide an attractive or repulsive force (typically on the order of piconewtons), depending on the relative refractive index between particle and surrounding medium, to physically hold and move microscopic objects similar to tweezers.

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Parkinson's disease

Parkinson's disease (PD) is a long-term degenerative disorder of the central nervous system that mainly affects the motor system.

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Peptide

Peptides (from Gr.: πεπτός, peptós "digested"; derived from πέσσειν, péssein "to digest") are short chains of amino acid monomers linked by peptide (amide) bonds.

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Peptide bond

A peptide bond is a covalent chemical bond linking two consecutive amino acid monomers along a peptide or protein chain.

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Peter Guy Wolynes

Peter Guy Wolynes is an American theoretical chemist and physicist.

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PH

In chemistry, pH is a logarithmic scale used to specify the acidity or basicity of an aqueous solution.

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Pharmacological chaperone

A pharmacological chaperone (or pharmacoperone, from "protein chaperone") is a small molecule that enters cells and serves as a molecular scaffolding in order to cause otherwise-misfolded mutant proteins to fold and route correctly within the cell.

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Phi value analysis

Phi value analysis, \phi analysis, or \phi-value analysis is an experimental protein engineering technique for studying the structure of the folding transition state of small protein domains that fold in a two-state manner.

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Physical change

Physical changes are changes affecting the form of a chemical substance, but not its chemical composition.

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Picosecond

A picosecond is an SI unit of time equal to 10−12 or 1/1,000,000,000,000 (one trillionth) of a second.

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Potential energy of protein

Internal potential energy of a molecule in molecular mechanics is described by a system of functions known as forced field.

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Precipitation (chemistry)

Precipitation is the creation of a solid from a solution.

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Prion

Prions are misfolded proteins that are associated with several fatal neurodegenerative diseases in animals and humans.

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Protein

Proteins are large biomolecules, or macromolecules, consisting of one or more long chains of amino acid residues.

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Protein biosynthesis

Protein synthesis is the process whereby biological cells generate new proteins; it is balanced by the loss of cellular proteins via degradation or export.

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Protein design

Protein design is the rational design of new protein molecules to design novel activity, behavior, or purpose, and to advance basic understanding of protein function.

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Protein domain

A protein domain is a conserved part of a given protein sequence and (tertiary) structure that can evolve, function, and exist independently of the rest of the protein chain.

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Protein dynamics

Proteins are generally thought to adopt unique structures determined by their amino acid sequences, as outlined by Anfinsen's dogma.

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Protein folding

Protein folding is the physical process by which a protein chain acquires its native 3-dimensional structure, a conformation that is usually biologically functional, in an expeditious and reproducible manner.

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Protein misfolding cyclic amplification

Protein misfolding cyclic amplification (PMCA) is an amplification technique (conceptually like PCR but not involving nucleotides) to multiply misfolded prions originally developed by Soto and colleagues.

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Protein primary structure

Protein primary structure is the linear sequence of amino acids in a peptide or protein.

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Protein quaternary structure

Protein quaternary structure is the number and arrangement of multiple folded protein subunits in a multi-subunit complex.

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Protein secondary structure

Protein secondary structure is the three dimensional form of local segments of proteins.

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Protein structure

Protein structure is the three-dimensional arrangement of atoms in an amino acid-chain molecule.

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Protein structure prediction

Protein structure prediction is the inference of the three-dimensional structure of a protein from its amino acid sequence—that is, the prediction of its folding and its secondary and tertiary structure from its primary structure.

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Protein tertiary structure

Protein tertiary structure is the three dimensional shape of a protein.

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Proteolysis

Proteolysis is the breakdown of proteins into smaller polypeptides or amino acids.

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Proteopathy

In medicine, proteopathy (Proteo-; -pathy; proteopathies pl.; proteopathic adj.) refers to a class of diseases in which certain proteins become structurally abnormal, and thereby disrupt the function of cells, tissues and organs of the body.

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Quantum yield

The quantum yield (Φ) of a radiation-induced process is the number of times a specific event occurs per photon absorbed by the system.

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Ramachandran plot

A Ramachandran plot (also known as a Ramachandran diagram or a plot), originally developed in 1963 by G. N. Ramachandran, C. Ramakrishnan, and V. Sasisekharan, is a way to visualize energetically allowed regions for backbone dihedral angles ψ against φ of amino acid residues in protein structure.

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Random coil

A random coil is a polymer conformation where the monomer subunits are oriented randomly while still being bonded to adjacent units.

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Reaction intermediate

A reaction intermediate or an intermediate is a molecular entity that is formed from the reactants (or preceding intermediates) and reacts further to give the directly observed products of a chemical reaction.

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Ribosome

The ribosome is a complex molecular machine, found within all living cells, that serves as the site of biological protein synthesis (translation).

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Rosetta@home

Rosetta@home is a distributed computing project for protein structure prediction on the Berkeley Open Infrastructure for Network Computing (BOINC) platform, run by the Baker laboratory at the University of Washington.

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Salt (chemistry)

In chemistry, a salt is an ionic compound that can be formed by the neutralization reaction of an acid and a base.

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Self-assembly

Self-assembly is a process in which a disordered system of pre-existing components forms an organized structure or pattern as a consequence of specific, local interactions among the components themselves, without external direction.

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Sheena Radford

Sheena Elizabeth Radford FRS FMedSci is a British biophysicist, and Astbury Professor of Biophysics in the Astbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology at the University of Leeds.

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Solubility

Solubility is the property of a solid, liquid or gaseous chemical substance called solute to dissolve in a solid, liquid or gaseous solvent.

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Solution

In chemistry, a solution is a special type of homogeneous mixture composed of two or more substances.

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Solvent

A solvent (from the Latin solvō, "loosen, untie, solve") is a substance that dissolves a solute (a chemically distinct liquid, solid or gas), resulting in a solution.

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Spontaneous process

A spontaneous process is the time-evolution of a system in which it releases free energy and it moves to a lower, more thermodynamically stable energy state.

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Stanford University

Stanford University (officially Leland Stanford Junior University, colloquially the Farm) is a private research university in Stanford, California.

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Statistical potential

In protein structure prediction, a statistical potential or knowledge-based potential is an energy function derived from an analysis of known protein structures in the Protein Data Bank.

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Stopped-flow

Stopped-flow is a lab technique for studying fast chemical reactions.

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Tafamidis

Tafamidis (trade name Vyndaqel) is a drug used to delay loss of peripheral nerve function in adults with familial amyloid polyneuropathy (FAP), an orphan disease.

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Temperature

Temperature is a physical quantity expressing hot and cold.

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Temperature jump

The temperature jump method is a technique used in chemical kinetics for the measurement of very rapid reaction rates.

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Thermodynamic free energy

The thermodynamic free energy is the amount of work that a thermodynamic system can perform.

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Thermostability

Thermostability is the quality of a substance to resist irreversible change in its chemical or physical structure, often by resisting decomposition or polymerization, at a high relative temperature.

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Three-dimensional space

Three-dimensional space (also: 3-space or, rarely, tri-dimensional space) is a geometric setting in which three values (called parameters) are required to determine the position of an element (i.e., point).

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Time-resolved mass spectrometry

Time-resolved mass spectrometry (TRMS) is a strategy in analytical chemistry that uses mass spectrometry platform to collect data with temporal resolution.

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Translation (biology)

In molecular biology and genetics, translation is the process in which ribosomes in the cytoplasm or ER synthesize proteins after the process of transcription of DNA to RNA in the cell's nucleus.

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Umbrella sampling

Umbrella sampling is a technique in computational physics and chemistry, used to improve sampling of a system (or different systems) where ergodicity is hindered by the form of the system's energy landscape.

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Van der Waals force

In molecular physics, the van der Waals forces, named after Dutch scientist Johannes Diderik van der Waals, are distance-dependent interactions between atoms or molecules.

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Vibrational circular dichroism

Vibrational circular dichroism (VCD) is a spectroscopic technique which detects differences in attenuation of left and right circularly polarized light passing through a sample.

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Von Willebrand factor

Von Willebrand factor (vWF) is a blood glycoprotein involved in hemostasis.

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Water

Water is a transparent, tasteless, odorless, and nearly colorless chemical substance that is the main constituent of Earth's streams, lakes, and oceans, and the fluids of most living organisms.

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X-ray crystallography

X-ray crystallography is a technique used for determining the atomic and molecular structure of a crystal, in which the crystalline atoms cause a beam of incident X-rays to diffract into many specific directions.

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References

[1] https://en.wikipedia.org/wiki/Protein_folding

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