13C NMR of study of entrapping proteins (α-chymotrypsin) into reversed micelles of surfactants (aerosol OT) in organic solvents (n-octane)

Autor:	Nikolai A. Budanov, Nataliya L. Klyachko, Yurii E. Shapiro, Andrei V. Levashov, Karel Martinek, Yurii L. Khmelnitsky
Rok vydání:	1989
Předmět:	Chymotrypsin Immobilized enzyme biology Chemistry Relaxation (NMR) General Chemistry Carbon-13 NMR Micelle chemistry.chemical_compound Polymer chemistry biology.protein Organic chemistry Molecule Spectroscopy Octane
Zdroj:	Collection of Czechoslovak Chemical Communications. 54:1126-1134
ISSN:	1212-6950 0010-0765
DOI:	10.1135/cccc19891126
Popis:	Hydrated reversed micelles of Aerosol OT (AOT) in octane have been studied by 13C NMR spectroscopy. The changes of spin-lattice relaxation times (T1) for individual segments of the AOT molecule, induced by entrapping a protein (α-chymotrypsin) into the micelle, have been determined by the inversion-recovery technique. The dramatic (three-fold) increase of T1 found for the α-CH2 groups in the AOT molecules indicates that (unlike in the unfilled micelle) in the protein-containing micelle the boundary of the water cavity is shifted outward (0.5-0.7 nm, under the given experimental conditions), the alkyl chains of the surfactant being “flooded” by water molecules. This observation explains why the outer size of the reversed micelle does not change on insertion of a bulky protein molecule.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::41d6a91e65e048454dd9a0471e1748ea https://doi.org/10.1135/cccc19891126 Zobrazit plný text záznamu