Thermodynamics and kinetics of protein folding

1995 ◽  
pp. 199-213
Author(s):  
Andrej Sali ◽  
Eugene Shakhnovich ◽  
Martin Karplus
Keyword(s):  
Protein Folding ◽  
Thermodynamics And Kinetics ◽  
Kinetics Of

Macromolecular conformations and interactions

2018 ◽  
Author(s):  
Dennis Sherwood ◽  
Paul Dalby
Keyword(s):  
Amino Acids ◽  
Free Energy ◽  
Protein Folding ◽  
Energy Minimum ◽  
Huge Number ◽  
Thermodynamics And Kinetics ◽  
Ligand Interactions ◽  
Kinetics Of ◽  
Single Configuration ◽  
Over Time

As a polymer of many amino acids, any given protein can, in principle, adopt a huge number of configurations. In reality, however, the biologically stable protein adopts a single configuration that is stable over time. Thermodynamically, this configuration must represent a Gibbs free energy minimum. This chapter therefore explores how the thermodynamics and kinetics of protein folding and unfolding can be investigated experimentally (using, for example, chaotropes, heating or ligand interactions), and how these measurements can be used to enrich our understanding of protein configurations and stability.

Thermodynamics and kinetics of protein folding: A mean field theory

2003 ◽  
Vol 5 (23) ◽  
pp. 5300 ◽  
Author(s):  
Kuo Kan Liang ◽  
Michitoshi Hayashi ◽  
YingJen Shiu ◽  
Yan Mo ◽  
Jiushu Shao ◽  
...  
Keyword(s):  
Field Theory ◽  
Protein Folding ◽  
Mean Field Theory ◽  
Mean Field ◽  
Thermodynamics And Kinetics ◽  
Kinetics Of

scholarly journals Topography of funneled landscapes determines the thermodynamics and kinetics of protein folding

2012 ◽  
Vol 109 (39) ◽  
pp. 15763-15768 ◽  
Author(s):  
J. Wang ◽  
R. J. Oliveira ◽  
X. Chu ◽  
P. C. Whitford ◽  
J. Chahine ◽  
...  
Keyword(s):  
Protein Folding ◽  
Thermodynamics And Kinetics ◽  
Kinetics Of

FOLDING SIMULATIONS FOR A THREE-HELIX BUNDLE PROTEIN

2003 ◽  
Vol 17 (01n02) ◽  
pp. 49-54 ◽  
Author(s):  
LONGHUA HU ◽  
JUN WANG ◽  
WEI WANG
Keyword(s):  
Protein Folding ◽  
Dihedral Angle ◽  
Lattice Model ◽  
Helix Bundle ◽  
Thermodynamics And Kinetics ◽  
Wide Range ◽  
Folding Simulations ◽  
Kinetics Of ◽  
Folding Thermodynamics ◽  
Bundle Protein

The folding thermodynamics and kinetics of a three-helix bundle protein with off-lattice model are studied using Monter Carlo simulations over a wide range of temperatures. By varying the strength of the dihedral angle potential, the effect of dihedral angle in folding is examined and it is demonstrated that the dihedral angle potential has much influence on protein folding thermodynamics and kinetics.

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