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Volumn 11, Issue 2, 2002, Pages 221-232

Rapid structural fluctuations of the free HIV protease flaps in solution: Relationship to crystal structures and comparison with predictions of dynamics calculations

Author keywords

AIDS; Hydrogen bonds; NMR; Relaxation; Secondary structure

Indexed keywords

HYDROGEN; LIGAND; NITROGEN 15; PROTEINASE; VIRUS ENZYME;

EID: 0036147844     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.33202     Document Type: Article
Times cited : (192)

References (46)
  • 16
    • 0024551334 scopus 로고
    • Characterization of thermotropic state changes in myosin subfragment-1 and heavy meromyosin by UV difference spectroscopy
    • (1989) J. Biol. Chem. , vol.264 , pp. 5586-5592
    • Kamath, U.1    Shriver, J.W.2
  • 22
    • 33646719091 scopus 로고
    • Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 1. Theory and range of validity
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 4546-4559
    • Lipari, G.1    Szabo, A.2
  • 23
    • 33845553743 scopus 로고
    • Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 2. Analysis of experimental results
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 4559-4570
    • Lipari, G.1    Szabo, A.2
  • 34
    • 0034483901 scopus 로고    scopus 로고
    • Curling of flap tips in HIV-1 protease as a mechanism for substrate entry and tolerance of drug resistance
    • (2000) Structure , vol.8 , pp. 1259-1265
    • Scott, W.R.P.1    Schiffer, C.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.