SCOPUS 정보 검색 플랫폼

Volumn 10, Issue 30, 2012, Pages 5887-5891

Ionization state of the catalytic dyad Asp25/25′ in the HIV-1 protease: NMR studies of site-specifically 13C labelled HIV-1 protease prepared by total chemical synthesis

(2) Torbeev, Vladimir Yu a Kent, Stephen B H a

a UNIVERSITY OF CHICAGO (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; CHEMICAL SYNTHESIS; ENZYME MOLECULES; HIV-1 PROTEASE; IONIZATION STATE; NMR MEASUREMENTS; NMR STUDIES; SIDE-CHAINS;

CHEMISTRY; POSITIVE IONS;

SYNTHESIS (CHEMICAL);

ASPARTIC ACID; CARBON; HUMAN IMMUNODEFICIENCY VIRUS PROTEINASE;

ARTICLE; BINDING SITE; BIOCATALYSIS; CHEMISTRY; ENZYME SPECIFICITY; ENZYMOLOGY; HUMAN IMMUNODEFICIENCY VIRUS 1; ISOTOPE LABELING; METABOLISM; MOLECULAR DYNAMICS; NUCLEAR MAGNETIC RESONANCE; PROTEIN CONFORMATION; SYNTHESIS;

ASPARTIC ACID; BINDING SITES; BIOCATALYSIS; CARBON ISOTOPES; CHEMISTRY TECHNIQUES, SYNTHETIC; HIV PROTEASE; HIV-1; ISOTOPE LABELING; MOLECULAR DYNAMICS SIMULATION; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN CONFORMATION; SUBSTRATE SPECIFICITY;

HUMAN IMMUNODEFICIENCY VIRUS 1;

EID: 84863883962 PISSN: 14770520 EISSN: None Source Type: Journal
DOI: 10.1039/c2ob25569c Document Type: Article

Times cited : (22)

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