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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 ...
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 A, B and C are isoforms encoded from the same gene through alternative splicing. A protein isoform, or "protein variant", [1] is a member of a set of highly similar proteins that originate from a single gene and are the result of genetic differences. [2] While many perform the same or similar biological roles, some isoforms have unique ...
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.
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 database normalization, unnormalized form (UNF or 0NF), also known as an unnormalized relation or non-first normal form (N1NF or NF 2), [1] is a database data model (organization of data in a database) which does not meet any of the conditions of database normalization defined by the relational model.
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 .
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]