Related ArticlesNMR relaxation studies of the role of conformational entropy in protein stability and ligand binding.
Acc Chem Res. 2001 May;34(5):379-88
Authors: Stone MJ
Recent advances in the measurement and analysis of protein NMR relaxation data have made it possible to characterize the dynamical properties of many backbone and side chain groups. With certain caveats, changes in flexibility that occur upon ligand binding, mutation, or changes in sample conditions can be interpreted in terms of contributions to conformational entropy. Backbone and side chain flexibility can either decrease or increase upon ligand binding. Decreases are often associated with "enthalpy-entropy compensation" and "induced fit" binding, whereas increases in conformational entropy can contribute to stabilization of complexes. In certain cases, conformational entropy appears to play a role in cooperative binding and enzyme catalysis. In addition, variations in conformational entropy and heat capacity may both be important in stabilizing the folded structures of proteins.
[NMR paper] CD and NMR studies of prion protein (PrP) helix 1. Novel implications for its role in
CD and NMR studies of prion protein (PrP) helix 1. Novel implications for its role in the PrPC-->PrPSc conversion process.
Related Articles CD and NMR studies of prion protein (PrP) helix 1. Novel implications for its role in the PrPC-->PrPSc conversion process.
J Biol Chem. 2003 Dec 12;278(50):50175-81
Authors: Ziegler J, Sticht H, Marx UC, Müller W, Rösch P, Schwarzinger S
The conversion of prion helix 1 from an alpha-helical into an extended conformation is generally assumed to be an essential step in the conversion of the cellular isoform...
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[NMR paper] Insights into the determinants of beta-sheet stability: 1H and 13C NMR conformational
Insights into the determinants of beta-sheet stability: 1H and 13C NMR conformational investigation of three-stranded antiparallel beta-sheet-forming peptides.
Related Articles Insights into the determinants of beta-sheet stability: 1H and 13C NMR conformational investigation of three-stranded antiparallel beta-sheet-forming peptides.
J Pept Res. 2003 Apr;61(4):177-88
Authors: Santiveri CM, Rico M, Jiménez MA, Pastor MT, Pérez-Payá E
In a previous study we designed a 20-residue peptide able to adopt a significant population of a three-stranded...
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[NMR paper] Role of entropy in protein thermostability: folding kinetics of a hyperthermophilic c
Role of entropy in protein thermostability: folding kinetics of a hyperthermophilic cold shock protein at high temperatures using 19F NMR.
Related Articles Role of entropy in protein thermostability: folding kinetics of a hyperthermophilic cold shock protein at high temperatures using 19F NMR.
Biochemistry. 2002 Oct 1;41(39):11670-80
Authors: Schuler B, Kremer W, Kalbitzer HR, Jaenicke R
We used (19)F NMR to extend the temperature range accessible to detailed kinetic and equilibrium studies of a hyperthermophilic protein. Employing an...
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[NMR paper] Comparison of protein backbone entropy and beta-sheet stability: NMR-derived dynamics
Comparison of protein backbone entropy and beta-sheet stability: NMR-derived dynamics of protein G B1 domain mutants.
Related Articles Comparison of protein backbone entropy and beta-sheet stability: NMR-derived dynamics of protein G B1 domain mutants.
J Am Chem Soc. 2001 Jan 10;123(1):185-6
Authors: Stone MJ, Gupta S, Snyder N, Regan L
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[NMR paper] NMR 15N relaxation and structural studies reveal slow conformational exchange in bars
NMR 15N relaxation and structural studies reveal slow conformational exchange in barstar C40/82A.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles NMR 15N relaxation and structural studies reveal slow conformational exchange in barstar C40/82A.
J Mol Biol. 1997 May 2;268(2):494-511
Authors: Wong KB, Fersht AR, Freund SM
Barstar an 89-residue protein consisting of four helices and a three-stranded parallel beta-sheet, is the intracellular inhibitor of the...
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[NMR paper] NMR 15N relaxation and structural studies reveal slow conformational exchange in bars
NMR 15N relaxation and structural studies reveal slow conformational exchange in barstar C40/82A.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles NMR 15N relaxation and structural studies reveal slow conformational exchange in barstar C40/82A.
J Mol Biol. 1997 May 2;268(2):494-511
Authors: Wong KB, Fersht AR, Freund SM
Barstar an 89-residue protein consisting of four helices and a three-stranded parallel beta-sheet, is the intracellular inhibitor of the...
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[NMR paper] Insights into the local residual entropy of proteins provided by NMR relaxation.
Insights into the local residual entropy of proteins provided by NMR relaxation.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Insights into the local residual entropy of proteins provided by NMR relaxation.
Protein Sci. 1996 Dec;5(12):2647-50
Authors: Li Z, Raychaudhuri S, Wand AJ
A simple model is used to...
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[NMR paper] Contributions to conformational entropy arising from bond vector fluctuations measure
Contributions to conformational entropy arising from bond vector fluctuations measured from NMR-derived order parameters: application to protein folding.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Contributions to conformational entropy arising from bond vector fluctuations measured from NMR-derived order parameters: application to protein folding.
J Mol Biol. 1996 Oct 25;263(2):369-82
Authors: Yang D, Kay LE
The relation between order parameters derived from NMR...