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44 relations: Amino acid, Biochemistry, Bioinformatics, Biological small-angle scattering, Biomolecular structure, Biomolecule, Biophysics, Cell (biology), Chaperonin, Circular dichroism, Cooperativity, Cryogenic electron microscopy, Denaturation (biochemistry), DNA, Dual-polarization interferometry, Electron paramagnetic resonance, Integral membrane protein, Macromolecule, Mass spectrometry, Membrane topology, Microscope, Molecular biology, Molecular model, Molecule, Multiangle light scattering, Native state, Nuclear magnetic resonance spectroscopy of proteins, Nucleic acid, Nucleic acid sequence, Protein, Protein Data Bank, Protein domain, Protein folding, Protein structure prediction, Protein subunit, Proteolysis, Proteopedia, Resolution (electron density), RNA, Stereochemistry, Structural genomics, Structural motif, Ultrafast laser spectroscopy, Wetting.
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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Biochemistry
Biochemistry, sometimes called biological chemistry, is the study of chemical processes within and relating to living organisms.
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Bioinformatics
Bioinformatics is an interdisciplinary field that develops methods and software tools for understanding biological data.
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Biological small-angle scattering
Biological small-angle scattering is a small-angle scattering method for structure analysis of biological materials.
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Biomolecular structure
Biomolecular structure is the intricate folded, three-dimensional shape that is formed by a molecule of protein, DNA, or RNA, and that is important to its function.
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Biomolecule
A biomolecule or biological molecule is a loosely used term for molecules and ions that are present in organisms, essential to some typically biological process such as cell division, morphogenesis, or development.
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Biophysics
Biophysics is an interdisciplinary science that applies the approaches and methods of physics to study biological systems.
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Cell (biology)
The cell (from Latin cella, meaning "small room") is the basic structural, functional, and biological unit of all known living organisms.
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Chaperonin
Chaperonins are proteins that provide favourable conditions for the correct folding of other proteins, thus preventing aggregation.
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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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Cooperativity
Cooperativity is a phenomenon displayed by systems involving identical or near-identical elements, which act dependently of each other, relative to a hypothetical standard non-interacting system in which the individual elements are acting independently.
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Cryogenic electron microscopy
Electron cryomicroscopy (CryoEM) is an electron microscopy (EM) technique where the sample is cooled to cryogenic temperatures.
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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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DNA
Deoxyribonucleic acid (DNA) is a thread-like chain of nucleotides carrying the genetic instructions used in the growth, development, functioning and reproduction of all known living organisms and many viruses.
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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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Electron paramagnetic resonance
Electron paramagnetic resonance (EPR) or electron spin resonance (ESR) spectroscopy is a method for studying materials with unpaired electrons.
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Integral membrane protein
An integral membrane protein (IMP) is a type of membrane protein that is permanently attached to the biological membrane.
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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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Mass spectrometry
Mass spectrometry (MS) is an analytical technique that ionizes chemical species and sorts the ions based on their mass-to-charge ratio.
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Membrane topology
Topology of a transmembrane protein refers to orientations (locations of N- and C-termini) of membrane-spanning segments with respect to the inner or outer sides of the biological membrane occupied by the protein.
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Microscope
A microscope (from the μικρός, mikrós, "small" and σκοπεῖν, skopeîn, "to look" or "see") is an instrument used to see objects that are too small to be seen by the naked eye.
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Molecular biology
Molecular biology is a branch of biology which concerns the molecular basis of biological activity between biomolecules in the various systems of a cell, including the interactions between DNA, RNA, proteins and their biosynthesis, as well as the regulation of these interactions.
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Molecular model
A molecular model, in this article, is a physical model that represents molecules and their processes.
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Molecule
A molecule is an electrically neutral group of two or more atoms held together by chemical bonds.
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Multiangle light scattering
Multiangle light scattering (MALS) describes a technique for measuring the light scattered by a sample into a plurality of angles.
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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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Nuclear magnetic resonance spectroscopy of proteins
Nuclear magnetic resonance spectroscopy of proteins (usually abbreviated protein NMR) is a field of structural biology in which NMR spectroscopy is used to obtain information about the structure and dynamics of proteins, and also nucleic acids, and their complexes.
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Nucleic acid
Nucleic acids are biopolymers, or small biomolecules, essential to all known forms of life.
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Nucleic acid sequence
A nucleic acid sequence is a succession of letters that indicate the order of nucleotides forming alleles within a DNA (using GACT) or RNA (GACU) molecule.
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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 Data Bank
The Protein Data Bank (PDB) is a crystallographic database for the three-dimensional structural data of large biological molecules, such as proteins and nucleic acids.
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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 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 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 subunit
In structural biology, a protein subunit is a single protein molecule that assembles (or "coassembles") with other protein molecules to form a protein complex.
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Proteolysis
Proteolysis is the breakdown of proteins into smaller polypeptides or amino acids.
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Proteopedia
Proteopedia is a wiki, 3D encyclopedia of proteins and other molecules.
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Resolution (electron density)
Resolution in terms of electron density is a measure of the resolvability in the electron density map of a molecule.
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RNA
Ribonucleic acid (RNA) is a polymeric molecule essential in various biological roles in coding, decoding, regulation, and expression of genes.
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Stereochemistry
Stereochemistry, a subdiscipline of chemistry, involves the study of the relative spatial arrangement of atoms that form the structure of molecules and their manipulation.
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Structural genomics
Structural genomics seeks to describe the 3-dimensional structure of every protein encoded by a given genome.
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Structural motif
In a chain-like biological molecule, such as a protein or nucleic acid, a structural motif is a supersecondary structure, which also appears in a variety of other molecules.
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Ultrafast laser spectroscopy
Ultrafast laser spectroscopy is a spectroscopic technique that uses ultrashort pulse lasers for the study of dynamics on extremely short time scales (attoseconds to nanoseconds).
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Wetting
Wetting is the ability of a liquid to maintain contact with a solid surface, resulting from intermolecular interactions when the two are brought together.
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References
[1] https://en.wikipedia.org/wiki/Structural_biology
