A solution NMR study of the binding kinetics and the internal dynamics of an HIV-1 protease-substrate complex

NMR studies of the binding of a substrate to an inactive HIV-1 protease construct, containing an active site mutation PR(D25N), are reported. Substrate titration measurements monitored by HSQC spectra and a (15)N-edited NOESY experiment show that the chromogenic substrate analog of the capsid/p2 cle...

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Hlavní autoři: Katoh, Etsuko, Louis, John M., Yamazaki, Toshimasa, Gronenborn, Angela M., Torchia, Dennis A., Ishima, Rieko
Médium: Artigo
Jazyk:Inglês
Vydáno: Wiley-Blackwell 2003
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On-line přístup:https://ncbi.nlm.nih.gov/pmc/articles/PMC2323926/
https://ncbi.nlm.nih.gov/pubmed/12824484
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