Fluctuating partially native-like topologies in the acid denatured ensemble of autolysis resistant HIV-1 protease

Archives of Biochemistry and Biophysics

Volumn 482, Issue 1-2, 2009, Pages 33-41

  Rout, Manoj Kumar ^a   Hosur, Ramakrishna V ^a  

^a TATA INSTITUTE OF FUNDAMENTAL RESEARCH   (India)

Author keywords

Acid denatured state; Backbone relaxation; HIV 1 protease; Hydrophobic clustering; Nuclear magnetic resonance; Secondary chemical shifts

Indexed keywords

ACETIC ACID; CYSTEINE; GUANIDINE; PROTEINASE; VIRUS ENZYME;

ARTICLE; AUTOLYSIS; CONCENTRATION PROCESS; CONTROLLED STUDY; DENATURATION; ENZYME ANALYSIS; ENZYME METABOLISM; HUMAN IMMUNODEFICIENCY VIRUS 1; HYDROPHOBICITY; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN SECONDARY STRUCTURE; SPECTROMETRY;

AUTOLYSIS; HIV PROTEASE; HIV-1; KINETICS; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; SPECTROSCOPY, FOURIER TRANSFORM INFRARED;

HUMAN IMMUNODEFICIENCY VIRUS 1;

EID: 58849166980     PISSN: 00039861     EISSN: 10960384     Source Type: Journal    
DOI: 10.1016/j.abb.2008.11.022     Document Type: Article

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