molecular biology, protein fold classes are broad categories of protein tertiary structure topology. They describe groups of proteins that share similar...

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...

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...

AlphaFold is an artificial intelligence (AI) program developed by DeepMind, a subsidiary of Alphabet, which performs predictions of protein structure....

proteins. There are multiple fold classes of globular proteins, since there are many different architectures that can fold into a roughly spherical shape...

predict protein folding and thus protein structure, for example, Itasser, and AlphaFold. AlphaFold was one of the first AIs to predict protein structures....

heme-containing globular proteins, involved in binding and/or transporting oxygen. These proteins all incorporate the globin fold, a series of eight alpha...

are proteins that assist the conformational folding or unfolding of large proteins or macromolecular protein complexes. There are a number of classes of...

assisting protein folding. HSP60 belong to a large class of molecules that assist protein folding, called molecular chaperones. Newly made proteins usually...

Small proteins are a diverse fold class of proteins (usually <100 amino acids long). Their tertiary structure is usually maintained by disulphide bridges...

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...

finger is a small protein structural motif that is characterized by the coordination of one or more zinc ions (Zn2+) which stabilizes the fold. The term zinc...

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...

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...

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...

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...

methods have a reasonable probability of predicting the folds of small, single-domain proteins within 1.5 angstroms over the entire structure. De novo...

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...

Membrane fusion proteins (not to be confused with chimeric or fusion proteins) are proteins that cause fusion of biological membranes. Membrane fusion...

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...

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...

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...

The thioredoxin fold is a protein fold common to enzymes that catalyze disulfide bond formation and isomerization. The fold is named for the canonical...

encode major capsid proteins that contain a single vertical jelly roll fold. All viruses in Singelaviria have two major capsid proteins (MCPs) that both...

elements typically spontaneously form as an intermediate before the protein folds into its three dimensional tertiary structure. Secondary structure is...

because proteins are the main functional units of the cell. Many proteins take on a defined configuration in a process known as protein folding in order...

organs of the body. Often the proteins fail to fold into their normal configuration; in this misfolded state, the proteins can become toxic in some way...

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...

pathways within cells that control the biogenesis, folding, trafficking, and degradation of proteins present within and outside the cell. Loss of proteostasis...

proteins that assist other proteins in assuming their three-dimensional fold, which is necessary for protein function. However, the fold of a protein...