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Real time NMR monitoring of local unfolding of HIV‐1 protease tethered dimer driven by autolysis
Author(s) -
Panchal Sanjay C.,
Bhavesh Neel S.,
Hosur R.V.
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)02426-7
Subject(s) - autolysis (biology) , dimer , chemistry , protein folding , protease , proteases , active site , hiv 1 protease , protein structure , biophysics , crystallography , ligand (biochemistry) , biochemistry , enzyme , biology , receptor , organic chemistry
Structural studies in proteases have been hampered because of their inherent autolytic function. However, since autolysis is known to be mediated via protein unfolding, careful monitoring of the autolytic reaction has the potential to throw light on the folding–unfolding equilibria. In this paper we describe real time nuclear magnetic resonance investigations on the tethered dimer construct of the human immunodeficiency virus‐1 protease, which have yielded insights into the relative stabilities of several residues in the protein. The residues lying along the active site (bottom, side and top of the active site) and those in helix have lower unfolding free energy values than the other parts of the protein. The residue level stability differences suggest that the protein is well suited to adjust itself in almost all the regions of its structure, as and when perturbations occur, either due to ligand binding or due to mutations.