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Journal Abstract Search


233 related items for PubMed ID: 16909839

  • 1. [Optimal relationship between average conformational entropy and average energy of interactions between residues for fast protein folding].
    Galzitskaia OV, Garbuzinskiĭ SA.
    Biofizika; 2006; 51(4):622-32. PubMed ID: 16909839
    [Abstract] [Full Text] [Related]

  • 2. Entropy capacity determines protein folding.
    Galzitskaya OV, Garbuzynskiy SO.
    Proteins; 2006 Apr 01; 63(1):144-54. PubMed ID: 16400647
    [Abstract] [Full Text] [Related]

  • 3. Optimal region of average side-chain entropy for fast protein folding.
    Galzitskaya OV, Surin AK, Nakamura H.
    Protein Sci; 2000 Mar 01; 9(3):580-6. PubMed ID: 10752620
    [Abstract] [Full Text] [Related]

  • 4. More compact protein globules exhibit slower folding rates.
    Galzitskaya OV, Reifsnyder DC, Bogatyreva NS, Ivankov DN, Garbuzynskiy SO.
    Proteins; 2008 Feb 01; 70(2):329-32. PubMed ID: 17876831
    [Abstract] [Full Text] [Related]

  • 5. The nature of the free energy barriers to two-state folding.
    Akmal A, Muñoz V.
    Proteins; 2004 Oct 01; 57(1):142-52. PubMed ID: 15326600
    [Abstract] [Full Text] [Related]

  • 6. [Radius of gyration is indicator of compactness of protein structure].
    Lobanov MIu, Bogatyreva NS, Galzitskaia OV.
    Mol Biol (Mosk); 2008 Oct 01; 42(4):701-6. PubMed ID: 18856071
    [Abstract] [Full Text] [Related]

  • 7. Folding with downhill behavior and low cooperativity of proteins.
    Zuo G, Wang J, Wang W.
    Proteins; 2006 Apr 01; 63(1):165-73. PubMed ID: 16416404
    [Abstract] [Full Text] [Related]

  • 8. Estimates of the loss of main-chain conformational entropy of different residues on protein folding.
    Pal D, Chakrabarti P.
    Proteins; 1999 Aug 15; 36(3):332-9. PubMed ID: 10409826
    [Abstract] [Full Text] [Related]

  • 9. Comparison between long-range interactions and contact order in determining the folding rate of two-state proteins: application of long-range order to folding rate prediction.
    Gromiha MM, Selvaraj S.
    J Mol Biol; 2001 Jun 29; 310(1):27-32. PubMed ID: 11419934
    [Abstract] [Full Text] [Related]

  • 10. Rotamer strain energy in protein helices - quantification of a major force opposing protein folding.
    Penel S, Doig AJ.
    J Mol Biol; 2001 Jan 26; 305(4):961-8. PubMed ID: 11162106
    [Abstract] [Full Text] [Related]

  • 11. Class-specific correlations between protein folding rate, structure-derived, and sequence-derived descriptors.
    Kuznetsov IB, Rackovsky S.
    Proteins; 2004 Feb 01; 54(2):333-41. PubMed ID: 14696195
    [Abstract] [Full Text] [Related]

  • 12. Inter-residue interactions in protein folding and stability.
    Gromiha MM, Selvaraj S.
    Prog Biophys Mol Biol; 2004 Oct 01; 86(2):235-77. PubMed ID: 15288760
    [Abstract] [Full Text] [Related]

  • 13. A fast method to sample real protein conformational space.
    Feldman HJ, Hogue CW.
    Proteins; 2000 May 01; 39(2):112-31. PubMed ID: 10737933
    [Abstract] [Full Text] [Related]

  • 14. Estimation of changes in side chain configurational entropy in binding and folding: general methods and application to helix formation.
    Lee KH, Xie D, Freire E, Amzel LM.
    Proteins; 1994 Sep 01; 20(1):68-84. PubMed ID: 7824524
    [Abstract] [Full Text] [Related]

  • 15. Integrated prediction of protein folding and unfolding rates from only size and structural class.
    De Sancho D, Muñoz V.
    Phys Chem Chem Phys; 2011 Oct 14; 13(38):17030-43. PubMed ID: 21670826
    [Abstract] [Full Text] [Related]

  • 16. Theoretical analysis on changes in thermodynamic quantities upon protein folding: essential role of hydration.
    Imai T, Harano Y, Kinoshita M, Kovalenko A, Hirata F.
    J Chem Phys; 2007 Jun 14; 126(22):225102. PubMed ID: 17581082
    [Abstract] [Full Text] [Related]

  • 17. Refinement of the long-range order parameter in predicting folding rates of two-state proteins.
    Harihar B, Selvaraj S.
    Biopolymers; 2009 Nov 14; 91(11):928-35. PubMed ID: 19603493
    [Abstract] [Full Text] [Related]

  • 18. Side-chain conformational entropy in protein folding.
    Doig AJ, Sternberg MJ.
    Protein Sci; 1995 Nov 14; 4(11):2247-51. PubMed ID: 8563620
    [Abstract] [Full Text] [Related]

  • 19. Nonrandom distribution of intramolecular contacts in native single-domain proteins.
    Mounce BC, Kurt N, Ellison PA, Cavagnero S.
    Proteins; 2009 May 01; 75(2):404-12. PubMed ID: 18831044
    [Abstract] [Full Text] [Related]

  • 20. Multiple contact network is a key determinant to protein folding rates.
    Gromiha MM.
    J Chem Inf Model; 2009 Apr 01; 49(4):1130-5. PubMed ID: 19338373
    [Abstract] [Full Text] [Related]


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