Related ArticlesRole 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 optimized incorporation strategy, the small cold shock protein from the bacterium Thermotoga maritima (TmCsp) was labeled with 5-fluorotryptophan. Although chaotropically induced unfolding transitions revealed a significant decrease in the stabilization free energy upon fluorine labeling, the protein's kinetic folding mechanism is conserved. Temperature- and guanidinium chloride-dependent equilibrium unfolding transitions monitored by (19)F NMR agree well with the results from optical spectroscopy, and provide a stringent test of the two-state folding character of TmCsp. Folding and unfolding rate constants at high temperatures were determined from the (19)F NMR spectra close to the midpoint of thermal unfolding by global line shape analysis. In combination with results from stopped-flow experiments at lower temperatures, they show that the folding rate constant of TmCsp and its temperature dependence closely resemble those of its mesophilic homologue from Bacillus subtilis, BsCspB. However, the unfolding rate constant of TmCsp is two orders of magnitude lower over the entire temperature range that was investigated. Consequently, the difference in conformational stability between the two proteins is solely due to the unfolding rate constant over a wide temperature range. A thermodynamic analysis points to an important role of entropic factors in the stabilization of TmCsp relative to its mesophilic homologues.
[NMR paper] Probing the binding entropy of ligand-protein interactions by NMR.
Probing the binding entropy of ligand-protein interactions by NMR.
Related Articles Probing the binding entropy of ligand-protein interactions by NMR.
Chembiochem. 2005 Sep;6(9):1585-91
Authors: Homans SW
nmrlearner
Journal club
0
12-01-2010 06:56 PM
[NMR paper] NMR relaxation studies of the role of conformational entropy in protein stability and
NMR relaxation studies of the role of conformational entropy in protein stability and ligand binding.
Related Articles NMR 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...
nmrlearner
Journal club
0
11-19-2010 08:32 PM
[NMR paper] Solution NMR structure of the cold-shock protein from the hyperthermophilic bacterium
Solution NMR structure of the cold-shock protein from the hyperthermophilic bacterium Thermotoga maritima.
Related Articles Solution NMR structure of the cold-shock protein from the hyperthermophilic bacterium Thermotoga maritima.
Eur J Biochem. 2001 May;268(9):2527-39
Authors: Kremer W, Schuler B, Harrieder S, Geyer M, Gronwald W, Welker C, Jaenicke R, Kalbitzer HR
Cold-shock proteins (Csps) are a subgroup of the cold-induced proteins preferentially expressed in bacteria and other organisms on reduction of the growth temperature below the...
nmrlearner
Journal club
0
11-19-2010 08:32 PM
[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
nmrlearner
Journal club
0
11-19-2010 08:32 PM
[NMR paper] Folding kinetics of the SH3 domain of PI3 kinase by real-time NMR combined with optic
Folding kinetics of the SH3 domain of PI3 kinase by real-time NMR combined with optical spectroscopy.
Related Articles Folding kinetics of the SH3 domain of PI3 kinase by real-time NMR combined with optical spectroscopy.
J Mol Biol. 1998 Feb 27;276(3):657-67
Authors: Guijarro JI, Morton CJ, Plaxco KW, Campbell ID, Dobson CM
The refolding kinetics of the chemically denatured SH3 domain of phosphatidylinositol 3'-kinase (PI3-SH3) have been monitored by real-time one-dimensional 1H NMR coupled with a variety of other biophysical techniques. These...
nmrlearner
Journal club
0
11-17-2010 11:06 PM
[NMR paper] Negative entropy of halothane binding to protein: 19F-NMR with a novel cell.
Negative entropy of halothane binding to protein: 19F-NMR with a novel cell.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Negative entropy of halothane binding to protein: 19F-NMR with a novel cell.
Biochim Biophys Acta. 1997 Mar 15;1334(2-3):117-22
Authors: Yoshida T, Tanaka M, Mori Y, Ueda I
An obvious difficulty of the study of binding of volatile anesthetics to proteins is to prevent loss of the ligand during the procedure. A novel NMR tube was designed that...
nmrlearner
Journal club
0
08-22-2010 03:31 PM
[NMR paper] Negative entropy of halothane binding to protein: 19F-NMR with a novel cell.
Negative entropy of halothane binding to protein: 19F-NMR with a novel cell.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Negative entropy of halothane binding to protein: 19F-NMR with a novel cell.
Biochim Biophys Acta. 1997 Mar 15;1334(2-3):117-22
Authors: Yoshida T, Tanaka M, Mori Y, Ueda I
An obvious difficulty of the study of binding of volatile anesthetics to proteins is to prevent loss of the ligand during the procedure. A novel NMR tube was designed that...
nmrlearner
Journal club
0
08-22-2010 03:03 PM
Postdoctoral position to study Protein-Protein Interactions and their role in Mechanisms of Signal Transduction using protein solution NMR/x-ray crystallography
Spincore.com are advertising a postdoc NMR position. It sounds pretty interesting.
"""
Postdoctoral position to study Protein-Protein Interactions and their role in Mechanisms of Signal Transduction using protein solution NMR /x-ray crystallography
Case Medical School, Cleveland, Ohio, USA
How are signaling events transmitted from one protein to another? To answer this question we are looking to add a postdoctoral co-workers to our interdisciplinary team. Our interest is to understand protein-protein interactions, protein structure and dynamics in the context of cell signaling...
Role of entropy in protein thermostability: folding kinetics of a hyperthermophilic c
Linear Mode
