Circular Dichroism Studies of Chymotrypsin and Its Derivatives

Autor:	Marguerite Volini, Peter Tobias
Rok vydání:	1969
Předmět:	chemistry.chemical_classification Circular dichroism Chymotrypsin biology Stereochemistry Kinetics Active site Cell Biology Biochemistry Enzyme Protein structure chemistry biology.protein sense organs Ultracentrifuge Binding site skin and connective tissue diseases Molecular Biology
Zdroj:	Journal of Biological Chemistry. 244:5105-5109
ISSN:	0021-9258
DOI:	10.1016/s0021-9258(18)63633-6
Popis:	The kinetics of the deacylation of trimethylacetyl chymotrypsin were followed by direct observation of changes in the circular dichroism spectrum of the enzymic protein itself. These changes result either from an alteration of the protein conformation or from direct perturbation of aromatic or cystinyl residues in the active site of the enzyme.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::d6a4afb45f3b52b84a5f8876adff5e6a https://doi.org/10.1016/s0021-9258(18)63633-6 Zobrazit plný text záznamu