메뉴 건너뛰기




Volumn 9, Issue 11, 2000, Pages 2232-2245

Trp42 rotamers report reduced flexibility when the inhibitor acetyl-pepstatin is bound to HIV-1 protease

Author keywords

500 ps molecular dynamics; Acrylamide quenching; Dihedral trajectories; Dynamics influenced by inhibitor; Ground state heterogeneity; Trp fluorescence; Trp rotamers

Indexed keywords

ACRYLAMIDE; APOENZYME; MONOMER; N ACETYLPEPSTATIN; PROTEIN DERIVATIVE; PROTEIN TRP42; PROTEINASE; TRYPTOPHAN; UNCLASSIFIED DRUG;

EID: 0034487443     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.9.11.2232     Document Type: Article
Times cited : (9)

References (57)
  • 3
    • 0027933583 scopus 로고
    • Unfolding pathway of apomyoglobin. Simultaneous characterization of acidic conformational states by frequency domain flourometry
    • (1994) J Mol Biol , vol.241 , pp. 103-109
    • Bismuto, E.1    Irace, G.2
  • 4
    • 0030610813 scopus 로고    scopus 로고
    • b transitions of tryptophan: Applications of theory and experimental observations to fluorescence of proteins
    • (1997) Methods Enzymol , vol.278 , pp. 113-150
    • Callis, P.R.1
  • 9
    • 0020825202 scopus 로고
    • Quenching-resolved emisson anisotropy studies with single and multitryptophan-containing proteins
    • (1983) Biophys J , vol.43 , pp. 323-334
    • Eftink, M.1
  • 17
    • 0024504824 scopus 로고
    • Confirmation that multiexponential fluorescence decay behavior of holoazurin originates from conformational heterogeneity
    • (1989) Biochemistry , vol.28 , pp. 3923-3934
    • Hutnik, C.M.1    Szabo, A.G.2
  • 25
    • 0015230409 scopus 로고
    • Solute perturbation of protein fluorescence. The quenching of the tryptophyl fluorescence of model compounds and of lysozyme by iodide ion
    • (1971) Biochemistry , vol.10 , pp. 3254-3263
    • Lehrer, S.S.1
  • 36
    • 0003840108 scopus 로고    scopus 로고
    • AQUA, Computer program
    • Department of NMR Spectroscopy, Bijvoet Center for Biomolecular Research, Utrecht University, The Netherlands
    • (1996)
    • Rullman, J.A.C.1
  • 42
    • 0029913459 scopus 로고    scopus 로고
    • Conformational stability and catalytic activity of HIV-1 protease are both enhanced at high salt concentration
    • (1996) J Biol Chem , vol.271 , pp. 5458-5463
    • Szeltner, Z.1    Polgár, L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.