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Journal Abstract Search

298 related items for PubMed ID: 11979278

  • 1. Understanding protein hydrogen bond formation with kinetic H/D amide isotope effects.
    Krantz BA, Srivastava AK, Nauli S, Baker D, Sauer RT, Sosnick TR.
    Nat Struct Biol; 2002 Jun; 9(6):458-63. PubMed ID: 11979278
    [Abstract] [Full Text] [Related]

  • 2. D/H amide kinetic isotope effects reveal when hydrogen bonds form during protein folding.
    Krantz BA, Moran LB, Kentsis A, Sosnick TR.
    Nat Struct Biol; 2000 Jan; 7(1):62-71. PubMed ID: 10625430
    [Abstract] [Full Text] [Related]

  • 3. Direct analysis of backbone-backbone hydrogen bond formation in protein folding transition states.
    Yang X, Wang M, Fitzgerald MC.
    J Mol Biol; 2006 Oct 20; 363(2):506-19. PubMed ID: 16963082
    [Abstract] [Full Text] [Related]

  • 4. Free energy determinants of secondary structure formation: I. alpha-Helices.
    Yang AS, Honig B.
    J Mol Biol; 1995 Sep 22; 252(3):351-65. PubMed ID: 7563056
    [Abstract] [Full Text] [Related]

  • 5. Kinetic isotope effects reveal the presence of significant secondary structure in the transition state for the folding of the N-terminal domain of L9.
    Sato S, Raleigh DP.
    J Mol Biol; 2007 Jul 06; 370(2):349-55. PubMed ID: 17512540
    [Abstract] [Full Text] [Related]

  • 6. Stabilisation of alpha-helices by site-directed mutagenesis reveals the importance of secondary structure in the transition state for acylphosphatase folding.
    Taddei N, Chiti F, Fiaschi T, Bucciantini M, Capanni C, Stefani M, Serrano L, Dobson CM, Ramponi G.
    J Mol Biol; 2000 Jul 14; 300(3):633-47. PubMed ID: 10884358
    [Abstract] [Full Text] [Related]

  • 7. Contribution of a buried hydrogen bond to lambda repressor folding kinetics.
    Myers JK, Oas TG.
    Biochemistry; 1999 May 25; 38(21):6761-8. PubMed ID: 10346896
    [Abstract] [Full Text] [Related]

  • 8. Equilibrium hydrogen exchange reveals extensive hydrogen bonded secondary structure in the on-pathway intermediate of Im7.
    Gorski SA, Le Duff CS, Capaldi AP, Kalverda AP, Beddard GS, Moore GR, Radford SE.
    J Mol Biol; 2004 Mar 12; 337(1):183-93. PubMed ID: 15001361
    [Abstract] [Full Text] [Related]

  • 9. Exploring structures in protein folding funnels with free energy functionals: the transition state ensemble.
    Shoemaker BA, Wang J, Wolynes PG.
    J Mol Biol; 1999 Apr 02; 287(3):675-94. PubMed ID: 10092467
    [Abstract] [Full Text] [Related]

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  • 11. Structural characterization of the transition state for folding of muscle acylphosphatase.
    Chiti F, Taddei N, van Nuland NA, Magherini F, Stefani M, Ramponi G, Dobson CM.
    J Mol Biol; 1998 Nov 06; 283(4):893-903. PubMed ID: 9790847
    [Abstract] [Full Text] [Related]

  • 12. Folding of amphipathic alpha-helices on membranes: energetics of helix formation by melittin.
    Ladokhin AS, White SH.
    J Mol Biol; 1999 Jan 29; 285(4):1363-9. PubMed ID: 9917380
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  • 15. An evolutionary bridge to a new protein fold.
    Cordes MH, Burton RE, Walsh NP, McKnight CJ, Sauer RT.
    Nat Struct Biol; 2000 Dec 29; 7(12):1129-32. PubMed ID: 11101895
    [Abstract] [Full Text] [Related]

  • 16. Folding at the speed limit.
    Yang WY, Gruebele M.
    Nature; 2003 May 08; 423(6936):193-7. PubMed ID: 12736690
    [Abstract] [Full Text] [Related]

  • 17. Hydrogen exchange studies of the Arc repressor: evidence for a monomeric folding intermediate.
    Burgering MJ, Hald M, Boelens R, Breg JN, Kaptein R.
    Biopolymers; 1995 Feb 08; 35(2):217-26. PubMed ID: 7696567
    [Abstract] [Full Text] [Related]

  • 18. Statistical and molecular dynamics studies of buried waters in globular proteins.
    Park S, Saven JG.
    Proteins; 2005 Aug 15; 60(3):450-63. PubMed ID: 15937899
    [Abstract] [Full Text] [Related]

  • 19. Secondary structure and oligomerization behavior of equilibrium unfolding intermediates of the lambda cro repressor.
    Fabian H, Fälber K, Gast K, Reinstädler D, Rogov VV, Naumann D, Zamyatkin DF, Filimonov VV.
    Biochemistry; 1999 Apr 27; 38(17):5633-42. PubMed ID: 10220352
    [Abstract] [Full Text] [Related]

  • 20. Effects of backbone modification on helical peptides: the reduced carbonyl modification.
    Chang CF, Zehfus MH.
    Biopolymers; 1998 Sep 27; 46(3):181-93. PubMed ID: 9699466
    [Abstract] [Full Text] [Related]

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