Rotamer strain energy in protein helices - Quantification of a major force opposing protein folding

Journal of Molecular Biology

Volumn 305, Issue 4, 2001, Pages 961-968

  Penel, Simon ^a   Doig, Andrew J ^a  

^a UNIVERSITY OF MANCHESTER   (United Kingdom)

Author keywords

Conformational entropy; Protein structure; Rotamer; Strain; helix

Indexed keywords

PROTEIN;

ARTICLE; CALCULATION; ENERGY; ENTROPY; FORCE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN FOLDING; PROTEIN STRUCTURE; ROTATION;

EID: 0035951299     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2000.4339     Document Type: Article

References (24)

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5. Side-chain conformational entropy in protein folding
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7. Strain in protein structures as viewed through nonrotameric side-chains: II. Effects upon ligand binding
8. Analysis of the steric strain in the polypeptide backbone of protein molecules
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13. Side-chain structures in the first turn of the α-helix
14. Position dependence of non-polar amino acid intrinsic helical propensities
15. Position dependence of amino acid intrinsic helical propensities II: Non-charged polar residues: Ser, Thr, Asn, and Gln
16. Empirical scale of side-chain conformational entropy in protein folding
17. Restart procedure for the conjugate gradient method
18. Amino acid preferences for specific locations at the ends of α helices
19. Free energies of amino acid side-chain rotamers in α-helices, β-sheets and α-helix N-caps
20. Determination of α-helix N1 energies by addition of N1, N2 and N3 preferences to helix-coil theory
21. Side-chains in native and random coil protein conformations. Analysis of NMR coupling constants and Χ1 torsion angle preferences
22. Structural and thermodynamic analysis of compensating mutations within the core of chicken egg white lysozyme
23. The measure of interior disorder in a folded protein and its contribution to stability