NMR identification of local structural preferences in HIV‐1 protease tethered heterodimer in 6 M guanidine hydrochloride

FEBS Letters

Mittal, Rohit¹  Panchal, Sanjay C²  Bhavesh, Neel S²  Hosur, Ramakrishna V² 

[1] Department of Biological Sciences, Tata Institute of Fundamental Research, Homi Bhabha Road, Mumbai 400 005, India;Department of Chemical Sciences, Tata Institute of Fundamental Research, Homi Bhabha Road, Mumbai 400 005, India

关键词: Human immunodeficiency virus-1 protease;    Denatured/unfolded protein;    Guanidine hydrochloride;    Backbone resonance assignment;    Nuclear magnetic resonance;    HNN;    HN(C)N;    Residual structural propensity;    NMR;    nuclear magnetic resonance;    HIV;    human immunodeficiency virus;    AIDS;    acquired immunodeficiency syndrome;    HSQC;    heteronuclear single quantum coherence;    TROSY;    transverse relaxation-optimized spectroscopy;   

DOI  :  10.1016/S0014-5793(01)03066-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Understanding protein folding requires complete characterization of all the states of the protein present along the folding pathways. For this purpose nuclear magnetic resonance (NMR) has proved to be a very powerful technique because of the great detail it can unravel regarding the structure and dynamics of protein molecules. We report here NMR identification of local structural preferences in human immunodeficiency virus-1 protease in the ‘unfolded state’. Analyses of the chemical shifts revealed the presence of local structural preferences many of which are native-like, and there are also some non-native structural elements. Three-bond H^N–H^α coupling constants that could be measured for some of the N-terminal and C-terminal residues are consistent with the native-like β-structure. Unusually shifted ¹⁵N and amide proton chemical shifts of residues adjacent to some prolines and tryptophans also indicate the presence of some structural elements. These conclusions are supported by amide proton temperature coefficients and nuclear Overhauser enhancement data. The locations of the residues exhibiting preferred structural propensities on the crystal structure of the protein, give useful insights into the folding mechanism of this protein.

【 授权许可】

Unknown