Related ArticlesNMR elucidation of early folding hierarchy in HIV-1 protease.
J Biol Chem. 2003 May 30;278(22):19980-5
Authors: Bhavesh NS, Sinha R, Mohan PM, Hosur RV
Folding studies on proteases by the conventional hydrogen exchange experiments are severely hampered because of interference from the autolytic reaction in the interpretation of the exchange data. We report here NMR identification of the hierarchy of early conformational transitions (folding propensities) in HIV-1 protease by systematic monitoring of the changes in the state of the protein as it is subjected to different degrees of denaturation by guanidine hydrochloride. Secondary chemical shifts, HN-Halpha coupling constants, 1H-15N nuclear Overhauser effects, and 15N transverse relaxation parameters have been used to report on the residual structural propensities, motional restrictions, conformational transitions, etc., and the data suggest that even under the strongest denaturing conditions (6 m guanidine) hydrophobic clusters as well as different native and non-native secondary structural elements are transiently formed. These constitute the folding nuclei, which include residues spanning the active site, the hinge region, and the dimerization domain. Interestingly, the proline residues influence the structural propensities, and the small amino acids, Gly and Ala, enhance the flexibility of the protein. On reducing the denaturing conditions, partially folded forms appear. The residues showing high folding propensities are contiguous along the sequence at many locations or are in close proximity on the native protein structure, suggesting a certain degree of local cooperativity in the conformational transitions. The dimerization domain, the flaps, and their hinges seem to exhibit the highest folding propensities. The data suggest that even the early folding events may involve many states near the surface of the folding funnel.
[NMR paper] Elucidation of the protein folding landscape by NMR.
Elucidation of the protein folding landscape by NMR.
Related Articles Elucidation of the protein folding landscape by NMR.
Methods Enzymol. 2005;394:299-321
Authors: Dyson HJ, Wright PE
NMR is one of the few experimental methods that can provide detailed insights into the structure and dynamics of unfolded and partly folded states of proteins. Mapping the protein folding landscape is of central importance to understanding the mechanism of protein folding. In addition, it is now recognized that many proteins are intrinsically unstructured in...
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[NMR paper] Early and late M intermediates in the bacteriorhodopsin photocycle: a solid-state NMR
Early and late M intermediates in the bacteriorhodopsin photocycle: a solid-state NMR study.
Related Articles Early and late M intermediates in the bacteriorhodopsin photocycle: a solid-state NMR study.
Biochemistry. 1998 Jun 2;37(22):8088-96
Authors: Hu JG, Sun BQ, Bizounok M, Hatcher ME, Lansing JC, Raap J, Verdegem PJ, Lugtenburg J, Griffin RG, Herzfeld J
To enforce vectorial proton transport in bacteriorhodopsin (bR), it is necessary that there be a change in molecular structure between deprotonation and reprotonation of the...
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[NMR paper] The solution NMR structure of glucosylated N-glycans involved in the early stages of
The solution NMR structure of glucosylated N-glycans involved in the early stages of glycoprotein biosynthesis and folding.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles The solution NMR structure of glucosylated N-glycans involved in the early stages of glycoprotein biosynthesis and folding.
EMBO J. 1997 Jul 16;16(14):4302-10
Authors: Petrescu AJ, Butters TD, Reinkensmeier G, Petrescu S, Platt FM, Dwek RA, Wormald MR
Glucosylated oligomannose N-linked...
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[NMR paper] Detection and characterization of an early folding intermediate of T4 lysozyme using
Detection and characterization of an early folding intermediate of T4 lysozyme using pulsed hydrogen exchange and two-dimensional NMR.
Related Articles Detection and characterization of an early folding intermediate of T4 lysozyme using pulsed hydrogen exchange and two-dimensional NMR.
Biochemistry. 1992 May 26;31(20):4749-56
Authors: Lu J, Dahlquist FW
Two-dimensional 1H-15N NMR techniques combined with pulsed hydrogen-deuterium exchange have been used to characterize the folding pathway of T4 lysozyme. In the unfolded state, there is little...
[NMR paper] The structure of the site on adenovirus early region 1A responsible for binding to TA
The structure of the site on adenovirus early region 1A responsible for binding to TATA-binding protein determined by NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-standard-jbc_full_free.gif Related Articles The structure of the site on adenovirus early region 1A responsible for binding to TATA-binding protein determined by NMR spectroscopy.
J Biol Chem. 1999 Feb 5;274(6):3503-12
Authors: Molloy DP, Smith KJ, Milner AE, Gallimore PH, Grand RJ
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NMR elucidation of early folding hierarchy in HIV-1 protease.
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