Entropy calculations on a reversibly folding peptide: Changes in solute free energy cannot explain folding behavior

Proteins: Structure, Function and Genetics

Volumn 43, Issue 1, 2001, Pages 45-56

  Schäfer, Heiko ^a   Daura, Xavier ^a   Mark, Alan E ^b   Van Gunsteren, Wilfred F ^a  

^a ETH ZURICH   (Switzerland)

^b UNIVERSITY OF GRONINGEN   (Netherlands)

Author keywords

[No Author keywords available]

Indexed keywords

HEPTAPEPTIDE;

ARTICLE; CALCULATION; CORRELATION FUNCTION; ENERGY; ENTHALPY; ENTROPY; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN STRUCTURE; STRUCTURE ANALYSIS; TEMPERATURE DEPENDENCE; THERMODYNAMICS; THERMOSTABILITY;

ENTROPY; MATHEMATICAL COMPUTING; MODELS, CHEMICAL; PEPTIDE FRAGMENTS; PROBABILITY; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEINS;

EID: 0035314075     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/1097-0134(20010401)43:1<45::AID-PROT1016>3.0.CO;2-N     Document Type: Article

References (21)

1. On the use of classical statistical mechanics in the treatment of polymer chain conformation
2. Method for estimating the configurational entropy of macromolecules
3. Entropy estimation from simulations of nondiffusive systems
4. Free energy determination of polypeptide conformations generated by molecular dynamics
5. Estimation of absolute and relative entropies of macromolecules using the covariance matrix
6. Absolute entropies from molecular dynamics simulation trajectories
7. Dominant forces in protein folding
8. Entropic barriers, transition states, funnels, and exponential protein folding kinetics: A simple model
9. Optimal region of average side-chain entropy for fast protein folding
10. Correlation between changes in nuclear magnetic resonance order parameters and conformational entropy: Molecular dynamics simulations of native and denatured staphylococcal nuclease
11. Entropy in protein folding and in protein - Protein interactions
12. Empirical scale of side-chain conformational entropy in protein folding
13. Free energy determinants of secondary structure formation: I. α-helices
14. Reversible peptide folding in solution by molecular dynamics simulation
15. The GROMOS biomolecular simulation program package
16. Probing the helical secondary structure of short-chain β-peptides
17. Folding-unfolding thermodynamics of a β-heptapeptide from equilibrium simulations
18. Decomposition of the free energy of a system in terms of specific interactions
19. When are free energy components meaningful?
20. Peptide folding simulations: No solvent required?