Entropy calculations on the molten globule state of a protein: Side-chain entropies of α-lactalbumin

Proteins: Structure, Function and Genetics

Volumn 46, Issue 2, 2002, Pages 215-224

  Schäfer, Heiko ^a   Smith, Lorna J ^b   Mark, Alan E ^c   Van Gunsteren, Wilfred F ^a  

^a ETH ZURICH   (Switzerland)

^b UNIVERSITY OF OXFORD   (United Kingdom)

^c UNIVERSITY OF GRONINGEN   (Netherlands)

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA LACTALBUMIN; FUNCTIONAL GROUP;

ACIDITY; ARTICLE; ATOM; CALCULATION; COVARIANCE; ENTROPY; LIQUID; MOLECULAR DYNAMICS; MOLECULAR MODEL; PRIORITY JOURNAL; PROTEIN TERTIARY STRUCTURE; SIMULATION;

ENTROPY; LACTALBUMIN; PROTEIN STRUCTURE, SECONDARY;

EID: 0036467064     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.1166     Document Type: Article

References (24)

1. Unfolded proteins, compact states and molten globules
2. Molten globule and protein folding
3. The molten globule state of α-lactalbumin
4. Side-chain conformational disorder in a molten globule: Molecular dynamics simulations of the A-state of human α-lactalbumin
5. Estimation of absolute and relative entropies of macromolecules using the covariance matrix
6. Absolute entropies from molecular dynamics simulation trajectories
7. Entropy calculations on a reversibly folding peptide: Changes in solute free energy cannot explain folding behaviour
8. Molecular dynamics simulations of human α-lactalbumin: Changes to the structural and dynamical properties of the protein at low pH
9. Crystal structure of human α-lactalbumin at 1.7 Å resolution
10. Dominant forces in protein folding
11. Empirical scale of side-chain conformational entropy in protein folding
12. Estimation of changes in side chain configurational entropy in binding and folding: General methods and application to helix formation
13. Biased probability Monte Carlo conformational searches and electrostatic calculations for peptides and proteins
14. Side-chain conformational entropy in protein folding
15. Free-energies of aminoacid side-chain rotamers in alpha-helices, beta-sheets and alpha-helix N-caps
16. Entropy in protein folding and in protein-protein interactions
17. Estimates of the loss of main-chain conformational entropy of different residues on protein folding
18. Side-chain conformational entropy in protein unfolded states
19. Optimal region of average side-chain entropy for fast protein folding
20. Configurational entropy of native proteins
21. Contributions to protein entropy and heat capacity from bond vector motions measured by NMR spin relaxation
22. Redistribution and loss of side-chain entropy upon formation of a calmodulin-peptide complex
23. Correlation between changes in nuclear magnetic resonance order parapemters and conformational entropy: Molecular dynamics simulations of native and denatured staphylococcal nuclease