molecular biology, protein fold classes are broad categories of protein tertiary structure topology. They describe groups of proteins that share similar...
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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...
76 KB (8,706 words) - 12:29, 14 December 2024
a protein. For simple proteins, it can be the entire protein. The broadest groups on SCOP version 1.75 are the protein fold classes. These classes group...
22 KB (2,564 words) - 19:34, 16 August 2024
predict protein folding and thus protein structure, for example, Itasser, and AlphaFold. AlphaFold was one of the first AIs to predict protein structures....
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Globin (redirect from Globin fold)
heme-containing globular proteins, involved in binding and/or transporting oxygen. These proteins all incorporate the globin fold, a series of eight alpha...
19 KB (2,067 words) - 22:39, 2 November 2024
are proteins that assist the conformational folding or unfolding of large proteins or macromolecular protein complexes. There are a number of classes of...
29 KB (3,499 words) - 02:11, 21 December 2024
AlphaFold is an artificial intelligence (AI) program developed by DeepMind, a subsidiary of Alphabet, which performs predictions of protein structure....
64 KB (5,731 words) - 03:55, 4 January 2025
proteins. There are multiple fold classes of globular proteins, since there are many different architectures that can fold into a roughly spherical shape...
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Zinc finger (redirect from Zinc-finger protein)
finger is a small protein structural motif that is characterized by the coordination of one or more zinc ions (Zn2+) which stabilizes the fold. It was originally...
42 KB (4,879 words) - 13:27, 9 October 2024
Small proteins are a diverse fold class of proteins (usually <100 amino acids long). Their tertiary structure is usually maintained by disulphide bridges...
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The jelly roll or Swiss roll fold is a protein fold or supersecondary structure composed of eight beta strands arranged in two four-stranded sheets. The...
27 KB (2,889 words) - 19:21, 10 December 2023
protein folding into a specific 3D structure that determines its activity. A linear chain of amino acid residues is called a polypeptide. A protein contains...
103 KB (10,813 words) - 10:10, 30 December 2024
Chaperonin (category Protein folding)
assisting protein folding. HSP60 belong to a large class of molecules that assist protein folding, called molecular chaperones. Newly made proteins usually...
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helix/beta sheet proteins. While most proteins adopt a single stable fold, a few proteins can rapidly interconvert between one or more folds. These are referred...
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identified as a peptide, rather than a protein. To be able to perform their biological function, proteins fold into one or more specific spatial conformations...
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In molecular biology, a protein domain is a region of a protein's polypeptide chain that is self-stabilizing and that folds independently from the rest...
71 KB (8,443 words) - 19:00, 15 August 2024
change can impact the protein's ability to function or to fold correctly. Misfolded proteins have a tendency to form dense protein clumps, which are often...
40 KB (4,349 words) - 13:44, 31 December 2024
Proteostasis (redirect from Protein homeostasis)
pathways within cells that control the biogenesis, folding, trafficking, and degradation of proteins present within and outside the cell. Loss of proteostasis...
25 KB (2,922 words) - 16:16, 10 January 2024
transcription, translation, post translational modifications, and protein folding. Proteins are made from amino acids. In humans, some amino acids can be...
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help of an MHC class I protein. Because MHC class I molecules present peptides derived from cytosolic proteins, the pathway of MHC class I presentation...
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residues within proteins as they fold. This allows proteins to quickly find the correct arrangement of disulfide bonds in their fully folded state, and therefore...
19 KB (1,936 words) - 16:09, 10 July 2024
transformer protein (TFP) also known as a metamorphic protein is a protein that can interconvert between two or more shapes (also known as folds) each having...
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and its sequence (termed protein redesign). Rational protein design approaches make protein-sequence predictions that will fold to specific structures....
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perform chaperone functions by stabilizing new proteins to ensure correct folding or by helping to refold proteins that were damaged by the cell stress. This...
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CATH database (category Protein folds)
The CATH Protein Structure Classification database is a free, publicly available online resource that provides information on the evolutionary relationships...
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Chemical chaperone (category Protein folding)
Chemical chaperones are a class of small molecules that function to enhance the folding and/or stability of proteins. Chemical chaperones are a broad and...
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TIM barrel (category Protein folds)
isomerase), also known as an alpha/beta barrel,: 252 is a conserved protein fold consisting of eight alpha helices (α-helices) and eight parallel beta...
46 KB (4,820 words) - 13:28, 10 September 2024
Evolution of molecular chaperones (category Protein folding)
proteins that assist other proteins in assuming their three-dimensional fold, which is necessary for protein function. However, the fold of a protein...
10 KB (1,217 words) - 01:09, 19 February 2024
expression. The AAA proteins contain two domains, an N-terminal alpha/beta domain that binds and hydrolyzes nucleotides (a Rossmann fold) and a C-terminal...
12 KB (1,352 words) - 03:31, 10 November 2024
classification notes that 20 distinct protein folds have phosphatase activity, and 10 of these contain protein phosphatases. The CC1 fold is the most common, and includes...
21 KB (2,520 words) - 00:54, 15 December 2024