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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]
In molecular biology, an intrinsically disordered protein (IDP) is a protein that lacks a fixed or ordered three-dimensional structure, [2] [3] [4] typically in the absence of its macromolecular interaction partners, such as other proteins or RNA.
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.
In medicine, proteinopathy ([pref. protein]; -pathy [suff. disease]; proteinopathies pl.; proteinopathic adj), or proteopathy, protein conformational disorder, or protein misfolding disease, is a class of diseases in which certain proteins become structurally abnormal, and thereby disrupt the function of cells, tissues and organs of the body.
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 .
When a nascent protein is being translated, HSP70 is able to associate with the hydrophobic regions of the protein to prevent faulty interactions until translation is complete. [24] Post-translational protein folding occurs in a cycle where the protein becomes bound/released from the chaperone allowing burying hydrophobic groups and aiding in ...
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 ...