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Journal Abstract Search

203 related items for PubMed ID: 16953598

  • 1. Simulated unfolded-state ensemble and the experimental NMR structures of villin headpiece yield similar wide-angle solution X-ray scattering profiles.
    Zagrovic B, Pande VS.
    J Am Chem Soc; 2006 Sep 13; 128(36):11742-3. PubMed ID: 16953598
    [Abstract] [Full Text] [Related]

  • 2. Comparing atomistic simulation data with the NMR experiment: how much can NOEs actually tell us?
    Zagrovic B, van Gunsteren WF.
    Proteins; 2006 Apr 01; 63(1):210-8. PubMed ID: 16425239
    [Abstract] [Full Text] [Related]

  • 3. NMR characterization of a peptide model provides evidence for significant structure in the unfolded state of the villin headpiece helical subdomain.
    Tang Y, Goger MJ, Raleigh DP.
    Biochemistry; 2006 Jun 06; 45(22):6940-6. PubMed ID: 16734429
    [Abstract] [Full Text] [Related]

  • 4. Folding of the villin headpiece subdomain from random structures. Analysis of the charge distribution as a function of pH.
    Ripoll DR, Vila JA, Scheraga HA.
    J Mol Biol; 2004 Jun 11; 339(4):915-25. PubMed ID: 15165859
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  • 5. Peptide models provide evidence for significant structure in the denatured state of a rapidly folding protein: the villin headpiece subdomain.
    Tang Y, Rigotti DJ, Fairman R, Raleigh DP.
    Biochemistry; 2004 Mar 23; 43(11):3264-72. PubMed ID: 15023077
    [Abstract] [Full Text] [Related]

  • 6. Characterization of protein fold by wide-angle X-ray solution scattering.
    Makowski L, Rodi DJ, Mandava S, Devarapalli S, Fischetti RF.
    J Mol Biol; 2008 Nov 14; 383(3):731-44. PubMed ID: 18786543
    [Abstract] [Full Text] [Related]

  • 7. Influence of multiple well defined conformations on small-angle scattering of proteins in solution.
    Heller WT.
    Acta Crystallogr D Biol Crystallogr; 2005 Jan 14; 61(Pt 1):33-44. PubMed ID: 15608373
    [Abstract] [Full Text] [Related]

  • 8. High-resolution crystal structures of villin headpiece and mutants with reduced F-actin binding activity.
    Meng J, Vardar D, Wang Y, Guo HC, Head JF, McKnight CJ.
    Biochemistry; 2005 Sep 13; 44(36):11963-73. PubMed ID: 16142894
    [Abstract] [Full Text] [Related]

  • 9. Resolving conflicting crystallographic and NMR models for solution-state DNA with solution X-ray diffraction.
    Zuo X, Tiede DM.
    J Am Chem Soc; 2005 Jan 12; 127(1):16-7. PubMed ID: 15631426
    [Abstract] [Full Text] [Related]

  • 10. Distribution of molecular size within an unfolded state ensemble using small-angle X-ray scattering and pulse field gradient NMR techniques.
    Choy WY, Mulder FA, Crowhurst KA, Muhandiram DR, Millett IS, Doniach S, Forman-Kay JD, Kay LE.
    J Mol Biol; 2002 Feb 08; 316(1):101-12. PubMed ID: 11829506
    [Abstract] [Full Text] [Related]

  • 11. Conformational distributions of unfolded polypeptides from novel NMR techniques.
    Meier S, Blackledge M, Grzesiek S.
    J Chem Phys; 2008 Feb 07; 128(5):052204. PubMed ID: 18266409
    [Abstract] [Full Text] [Related]

  • 12. Free-energy landscape of the villin headpiece in an all-atom force field.
    Herges T, Wenzel W.
    Structure; 2005 Apr 07; 13(4):661-8. PubMed ID: 15837204
    [Abstract] [Full Text] [Related]

  • 13. Predicting the effect of a point mutation on a protein fold: the villin and advillin headpieces and their Pro62Ala mutants.
    Piana S, Laio A, Marinelli F, Van Troys M, Bourry D, Ampe C, Martins JC.
    J Mol Biol; 2008 Jan 11; 375(2):460-70. PubMed ID: 18022635
    [Abstract] [Full Text] [Related]

  • 14. Use of MM-PB/SA in estimating the free energies of proteins: application to native, intermediates, and unfolded villin headpiece.
    Lee MR, Duan Y, Kollman PA.
    Proteins; 2000 Jun 01; 39(4):309-16. PubMed ID: 10813813
    [Abstract] [Full Text] [Related]

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  • 19. Comparison of X-ray and NMR structures: is there a systematic difference in residue contacts between X-ray- and NMR-resolved protein structures?
    Garbuzynskiy SO, Melnik BS, Lobanov MY, Finkelstein AV, Galzitskaya OV.
    Proteins; 2005 Jul 01; 60(1):139-47. PubMed ID: 15856480
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