Faster access than browser!Similarities between Protein and Protein–protein interaction
Protein and Protein–protein interaction have 39 things in common (in Unionpedia): Actin, Biochemistry, Biomolecular structure, C-terminus, Cell cycle, Cell nucleus, Conformational change, Cytoplasm, Cytoskeleton, Disulfide, Enzyme, Enzyme catalysis, Hemoglobin, Hydrogen bond, Hydrophobic effect, Insulin, Interactome, John Kendrew, Mass spectrometry, Membrane protein, Molecular dynamics, Myoglobin, Myosin, Nuclear magnetic resonance, Nucleic acid, Oligomer, Post-translational modification, Proline, Protein, Protein complex, ..., Protein structure, Protein subunit, Protein–protein interaction prediction, RNA, Signal transduction, Substrate (chemistry), Threonine, Two-hybrid screening, X-ray crystallography. Expand index (9 more) »
Actin
Actin is a family of globular multi-functional proteins that form microfilaments.
Actin and Protein · Actin and Protein–protein interaction ·
Biochemistry
Biochemistry, sometimes called biological chemistry, is the study of chemical processes within and relating to living organisms.
Biochemistry and Protein · Biochemistry and Protein–protein interaction ·
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.
Biomolecular structure and Protein · Biomolecular structure and Protein–protein interaction ·
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).
C-terminus and Protein · C-terminus and Protein–protein interaction ·
Cell cycle
The cell cycle or cell-division cycle is the series of events that take place in a cell leading to its division and duplication of its DNA (DNA replication) to produce two daughter cells.
Cell cycle and Protein · Cell cycle and Protein–protein interaction ·
Cell nucleus
In cell biology, the nucleus (pl. nuclei; from Latin nucleus or nuculeus, meaning kernel or seed) is a membrane-enclosed organelle found in eukaryotic cells.
Cell nucleus and Protein · Cell nucleus and Protein–protein interaction ·
Conformational change
In biochemistry, a conformational change is a change in the shape of a macromolecule, often induced by environmental factors.
Conformational change and Protein · Conformational change and Protein–protein interaction ·
Cytoplasm
In cell biology, the cytoplasm is the material within a living cell, excluding the cell nucleus.
Cytoplasm and Protein · Cytoplasm and Protein–protein interaction ·
Cytoskeleton
A cytoskeleton is present in all cells of all domains of life (archaea, bacteria, eukaryotes).
Cytoskeleton and Protein · Cytoskeleton and Protein–protein interaction ·
Disulfide
In chemistry, a disulfide refers to a functional group with the structure R−S−S−R′.
Disulfide and Protein · Disulfide and Protein–protein interaction ·
Enzyme
Enzymes are macromolecular biological catalysts.
Enzyme and Protein · Enzyme and Protein–protein interaction ·
Enzyme catalysis
Enzyme catalysis is the increase in the rate of a chemical reaction by the active site of a protein.
Enzyme catalysis and Protein · Enzyme catalysis and Protein–protein interaction ·
Hemoglobin
Hemoglobin (American) or haemoglobin (British); abbreviated Hb or Hgb, is the iron-containing oxygen-transport metalloprotein in the red blood cells of all vertebrates (with the exception of the fish family Channichthyidae) as well as the tissues of some invertebrates.
Hemoglobin and Protein · Hemoglobin and Protein–protein interaction ·
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.
Hydrogen bond and Protein · Hydrogen bond and Protein–protein interaction ·
Hydrophobic effect
The hydrophobic effect is the observed tendency of nonpolar substances to aggregate in an aqueous solution and exclude water molecules.
Hydrophobic effect and Protein · Hydrophobic effect and Protein–protein interaction ·
Insulin
Insulin (from Latin insula, island) is a peptide hormone produced by beta cells of the pancreatic islets; it is considered to be the main anabolic hormone of the body.
Insulin and Protein · Insulin and Protein–protein interaction ·
Interactome
In molecular biology, an interactome is the whole set of molecular interactions in a particular cell.
Interactome and Protein · Interactome and Protein–protein interaction ·
John Kendrew
Sir John Cowdery Kendrew, (24 March 1917 – 23 August 1997) was an English biochemist and crystallographer who shared the 1962 Nobel Prize in Chemistry with Max Perutz; their group in the Cavendish Laboratory investigated the structure of heme-containing proteins.
John Kendrew and Protein · John Kendrew and Protein–protein interaction ·
Mass spectrometry
Mass spectrometry (MS) is an analytical technique that ionizes chemical species and sorts the ions based on their mass-to-charge ratio.
Mass spectrometry and Protein · Mass spectrometry and Protein–protein interaction ·
Membrane protein
Membrane proteins are proteins that interact with, or are part of, biological membranes.
Membrane protein and Protein · Membrane protein and Protein–protein interaction ·
Molecular dynamics
Molecular dynamics (MD) is a computer simulation method for studying the physical movements of atoms and molecules.
Molecular dynamics and Protein · Molecular dynamics and Protein–protein interaction ·
Myoglobin
Myoglobin (symbol Mb or MB) is an iron- and oxygen-binding protein found in the muscle tissue of vertebrates in general and in almost all mammals.
Myoglobin and Protein · Myoglobin and Protein–protein interaction ·
Myosin
Myosins are a superfamily of motor proteins best known for their roles in muscle contraction and in a wide range of other motility processes in eukaryotes.
Myosin and Protein · Myosin and Protein–protein interaction ·
Nuclear magnetic resonance
Nuclear magnetic resonance (NMR) is a physical phenomenon in which nuclei in a magnetic field absorb and re-emit electromagnetic radiation.
Nuclear magnetic resonance and Protein · Nuclear magnetic resonance and Protein–protein interaction ·
Nucleic acid
Nucleic acids are biopolymers, or small biomolecules, essential to all known forms of life.
Nucleic acid and Protein · Nucleic acid and Protein–protein interaction ·
Oligomer
An oligomer (oligo-, "a few" + -mer, "parts") is a molecular complex of chemicals that consists of a few monomer units, in contrast to a polymer, where the number of monomers is, in principle, infinite.
Oligomer and Protein · Oligomer and Protein–protein interaction ·
Post-translational modification
Post-translational modification (PTM) refers to the covalent and generally enzymatic modification of proteins following protein biosynthesis.
Post-translational modification and Protein · Post-translational modification and Protein–protein interaction ·
Proline
Proline (symbol Pro or P) is a proteinogenic amino acid that is used in the biosynthesis of proteins.
Proline and Protein · Proline and Protein–protein interaction ·
Protein
Proteins are large biomolecules, or macromolecules, consisting of one or more long chains of amino acid residues.
Protein and Protein · Protein and Protein–protein interaction ·
Protein complex
A protein complex or multiprotein complex is a group of two or more associated polypeptide chains.
Protein and Protein complex · Protein complex and Protein–protein interaction ·
Protein structure
Protein structure is the three-dimensional arrangement of atoms in an amino acid-chain molecule.
Protein and Protein structure · Protein structure and Protein–protein interaction ·
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.
Protein and Protein subunit · Protein subunit and Protein–protein interaction ·
Protein–protein interaction prediction
Protein–protein interaction prediction is a field combining bioinformatics and structural biology in an attempt to identify and catalog physical interactions between pairs or groups of proteins.
Protein and Protein–protein interaction prediction · Protein–protein interaction and Protein–protein interaction prediction ·
RNA
Ribonucleic acid (RNA) is a polymeric molecule essential in various biological roles in coding, decoding, regulation, and expression of genes.
Protein and RNA · Protein–protein interaction and RNA ·
Signal transduction
Signal transduction is the process by which a chemical or physical signal is transmitted through a cell as a series of molecular events, most commonly protein phosphorylation catalyzed by protein kinases, which ultimately results in a cellular response.
Protein and Signal transduction · Protein–protein interaction and Signal transduction ·
Substrate (chemistry)
In chemistry, a substrate is typically the chemical species being observed in a chemical reaction, which reacts with a reagent to generate a product.
Protein and Substrate (chemistry) · Protein–protein interaction and Substrate (chemistry) ·
Threonine
Threonine (symbol Thr or T) is an amino acid that is used in the biosynthesis of proteins.
Protein and Threonine · Protein–protein interaction and Threonine ·
Two-hybrid screening
Two-hybrid screening (originally known as yeast two-hybrid system or Y2H) is a molecular biology technique used to discover protein–protein interactions (PPIs) and protein–DNA interactions by testing for physical interactions (such as binding) between two proteins or a single protein and a DNA molecule, respectively.
Protein and Two-hybrid screening · Protein–protein interaction and Two-hybrid screening ·
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.
Protein and X-ray crystallography · Protein–protein interaction and X-ray crystallography ·
The list above answers the following questions
- What Protein and Protein–protein interaction have in common
- What are the similarities between Protein and Protein–protein interaction
Protein and Protein–protein interaction Comparison
Protein has 343 relations, while Protein–protein interaction has 127. As they have in common 39, the Jaccard index is 8.30% = 39 / (343 + 127).
References
This article shows the relationship between Protein and Protein–protein interaction. To access each article from which the information was extracted, please visit:
