Ad
related to: beta sandwich folds pdf notes worksheetgenerationgenius.com has been visited by 10K+ users in the past month
Search results
Results From The WOW.Com Content Network
Beta-sandwich or β-sandwich domains consisting of 80 to 350 amino acids occur commonly in proteins. They are characterized by two opposing antiparallel beta sheets (β-sheets). [ 1 ] The number of strands found in such domains may differ from one protein to another. β-sandwich domains are subdivided in a variety of different folds.
The fold to which a domain belongs is determined by inspection, rather than by software. The levels of SCOP version 1.75 are as follows. Class: Types of folds, e.g., beta sheets. Fold: The different shapes of domains within a class. Superfamily: The domains in a fold are grouped into superfamilies, which have at least a distant common ancestor.
In molecular biology, protein fold classes are broad categories of protein tertiary structure topology. They describe groups of proteins that share similar amino acid and secondary structure proportions.
The Rossmann fold is a tertiary fold found in proteins that bind nucleotides, such as enzyme cofactors FAD, NAD +, and NADP +.This fold is composed of alternating beta strands and alpha helical segments where the beta strands are hydrogen bonded to each other forming an extended beta sheet and the alpha helices surround both faces of the sheet to produce a three-layered sandwich.
The immunoglobulin domain, also known as the immunoglobulin fold, is a type of protein domain that consists of a 2-layer sandwich of 7-9 antiparallel β-strands arranged in two β-sheets with a Greek key topology, [1] [2] consisting of about 125 amino acids. The backbone switches repeatedly between the two β-sheets.
The fold is an elaboration on the Greek key motif and is sometimes considered a form of beta barrel. It is very common in viral proteins, particularly viral capsid proteins. [3] [4] Taken together, the jelly roll and Greek key structures comprise around 30% of the all-beta proteins annotated in the Structural Classification of Proteins (SCOP ...
All beta-barrels can be classified in terms of two integer parameters: the number of strands in the beta-sheet, n, and the "shear number", S, a measure of the stagger of the strands in the beta-sheet. [3] These two parameters (n and S) are related to the inclination angle of the beta strands relative to the axis of the barrel. [4] [5] [6]
The TIM barrel (triose-phosphate isomerase), also known as an alpha/beta barrel, [1]: 252 is a conserved protein fold consisting of eight alpha helices (α-helices) and eight parallel beta strands (β-strands) that alternate along the peptide backbone. [2] The structure is named after triose-phosphate isomerase, a conserved metabolic enzyme. [3]