Zobrazeno 1 - 3
of 3
pro vyhledávání: '"Beáta Ullrich"'
Autor:
Monique Laberge, Michel Vincent, Judit Fidy, László Polgár, Zoltán Szeltner, Beáta Ullrich, Jacques Gallay
Publikováno v:
Pure and Applied Chemistry. 73:415-419
The binding of acetylpepstatin to the Q7K/L33I/L63I mutant of HIV-1 protease was studied by fluorescence, phosphorescence, and 500-ps molecular dynamics. The protease is a homodimer with two tryptophans per monomer. Maximum entropy method (MEM) ana
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0aa0e4822fe8fcf76a8e667ccb15fe9a
https://doi.org/10.1351/pac200173030415
https://doi.org/10.1351/pac200173030415
Publikováno v:
Protein Science. 9:2232-2245
The Q7K/L331/L631 HIV-1 protease mutant was expressed in Escherichia coli and the effect of binding a substrate-analog inhibitor, acetyl-pepstatin, was investigated by fluorescence spectroscopy and molecular dynamics. The dimeric enzyme has four intr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::214f622ad2dd839d21a7832853e3d501
https://doi.org/10.1110/ps.9.11.2232
https://doi.org/10.1110/ps.9.11.2232
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1435:1-6
The Arrhenius plot of the de-excitation rate of tryptophan triplet state deviates from linearity in the physiological temperature range for several proteins with buried tryptophans, similarly to the behaviour of enzyme activity. A model is presented
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5d25a9fc758ddcf680a3a4c5dd628c63
https://doi.org/10.1016/s0167-4838(99)00200-9
https://doi.org/10.1016/s0167-4838(99)00200-9