[The volume and structure of the chymotrypsin active site]

Autor:	P V, Kostetskiĭ
Rok vydání:	2005
Předmět:	Models Molecular Binding Sites Animals Chymotrypsin Water Protein Structure Tertiary
Zdroj:	Biofizika. 50(6)
ISSN:	0006-3029
Popis:	It was found that the chymotrypsin active site is located in the largest cleft on the enzyme surface approximated by a sphere with a radius of 20 angstroms. The active site cleft volume is about 2 nm3, as computed by the Monte-Carlo method. The size and shape of the active site cleft-- the intersection of two unequal spheres--are sufficient for large (about 1 nm3) fragments of substrate molecules to enter the active site. The active site bottom and the adjacent narrow section are about 600 angstroms3 in volume and may serve as a combustion chamber of a water-substrate mixture during the operation of the enzyme machinery. Intrinsic water molecules inside the combustion chamber can take part in heat exchange during different steps of the enzymatic process.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=pmid________::4df8d7147f61bcf549afc0824c69f658 https://pubmed.ncbi.nlm.nih.gov/16358776 Zobrazit plný text záznamu