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Generally, the carbohydrate part(s) play an integral role in the function of a glycoconjugate; prominent examples of this are neural cell adhesion molecule (NCAM) and blood proteins where fine details in the carbohydrate structure determine cell binding (or not) or lifetime in circulation.
A protein structure database is a database that is modeled around the various experimentally determined protein structures. The aim of most protein structure databases is to organize and annotate the protein structures, providing the biological community access to the experimental data in a useful way.
Folded, 3-D structure of ribonuclease A. Anfinsen's dogma, also known as the thermodynamic hypothesis, is a postulate in molecular biology.It states that, at least for a small globular protein in its standard physiological environment, the native structure is determined only by the protein's amino acid sequence. [1]
Class III β-tubulin is a microtubule element expressed exclusively in neurons, [28] and is a popular identifier specific for neurons in nervous tissue. It binds colchicine much more slowly than other isotypes of β-tubulin. [29] β1-tubulin, sometimes called class VI β-tubulin, [30] is the most divergent at the amino acid sequence level. [31]
Protein tertiary structure can be divided into four main classes based on the secondary structural content of the domain. [25] All-α domains have a domain core built exclusively from α-helices. This class is dominated by small folds, many of which form a simple bundle with helices running up and down.
Cadherins are a class of type-1 transmembrane proteins, and they depend on calcium (Ca 2+) ions to function, hence their name. Cell-cell adhesion is mediated by extracellular cadherin domains, whereas the intracellular cytoplasmic tail associates with numerous adaptors and signaling proteins, collectively referred to as the cadherin adhesome .
Leucine zippers are present in both eukaryotic and prokaryotic regulatory proteins, but are mainly a feature of eukaryotes. They can also be annotated simply as ZIPs, and ZIP-like motifs have been found in proteins other than transcription factors and are thought to be one of the general protein modules for protein–protein interactions. [5]
Metalloprotein is a generic term for a protein that contains a metal ion cofactor. [1] [2] A large proportion of all proteins are part of this category. For instance, at least 1000 human proteins (out of ~20,000) contain zinc-binding protein domains [3] although there may be up to 3000 human zinc metalloproteins. [4]