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18091 Ensembl ENSG00000183072 ENSMUSG00000015579 UniProt P52952 P42582 RefSeq (mRNA) NM_004387 NM_001166175 NM_001166176 NM_008700 RefSeq (protein) NP_001159647 NP_001159648 NP_004378 NP_032726 Location (UCSC) Chr 5: 173.23 – 173.24 Mb Chr 17: 27.06 – 27.06 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Homeobox protein Nkx-2.5 is a protein that in humans is encoded by the NKX2 ...
Protein before and after folding Results of protein folding. Protein folding is the physical process by which a protein, after synthesis by a ribosome as a linear chain of amino acids, changes from an unstable random coil into a more ordered three-dimensional structure. This structure permits the protein to become biologically functional. [1]
Anisotrpic Network Model use an elastic mass-and-spring network to represent biological macromolecule (Elastic Network Model)The Anisotropic Network Model (ANM) is a simple yet powerful tool made for normal mode analysis of proteins, which has been successfully applied for exploring the relation between function and dynamics for many proteins.
Protein anabolism is the process by which proteins are formed from amino acids. It relies on five processes: amino acid synthesis, transcription , translation , post translational modifications , and protein folding .
In biochemistry, denaturation is a process in which proteins or nucleic acids lose folded structure present in their native state due to various factors, including 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), agitation and radiation, or heat. [3]
Protein structure is the three-dimensional arrangement of atoms in an amino acid-chain molecule. Proteins are polymers – specifically polypeptides – formed from ...
The presence of multiple domains in proteins gives rise to a great deal of flexibility and mobility, leading to protein domain dynamics. [1] Domain motions can be inferred by comparing different structures of a protein (as in Database of Molecular Motions ), or they can be directly observed using spectra [ 13 ] [ 2 ] measured by neutron spin ...
In contrast, C-reactive protein (with a half-life of 6–8 hours) rises rapidly and can quickly return to within the normal range if treatment is employed. For example, in active systemic lupus erythematosus, one may find a raised ESR but normal C-reactive protein. [citation needed] They may also indicate liver failure. [11]