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Journal Abstract Search

219 related items for PubMed ID: 17512540

  • 41.
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  • 44. Mutational investigation of protein folding transition states by Phi-value analysis and beyond: lessons from SH3 domain folding.
    Zarrine-Afsar A, Lin SL, Neudecker P.
    Biochem Cell Biol; 2010 Apr; 88(2):231-8. PubMed ID: 20453926
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  • 45.
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  • 46. Characterization of the hydrodynamic properties of the folding transition state of an SH3 domain by magnetization transfer NMR spectroscopy.
    Tollinger M, Neale C, Kay LE, Forman-Kay JD.
    Biochemistry; 2006 May 23; 45(20):6434-45. PubMed ID: 16700554
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  • 48. The folding transition state of the cold shock protein is strongly polarized.
    Garcia-Mira MM, Boehringer D, Schmid FX.
    J Mol Biol; 2004 Jun 04; 339(3):555-69. PubMed ID: 15147842
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  • 49. [On the role of some conserved and nonconserved amino acid residues in transition state and in intermediate of apomyoglobin folding].
    Baryshnikova EN, Mel'nik BS, Katina NS, Finkel'shteĭn AV, Bychkova VE.
    Mol Biol (Mosk); 2009 Jun 04; 43(1):136-47. PubMed ID: 19334536
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  • 50. The structure of the major transition state for folding of an FF domain from experiment and simulation.
    Jemth P, Day R, Gianni S, Khan F, Allen M, Daggett V, Fersht AR.
    J Mol Biol; 2005 Jul 08; 350(2):363-78. PubMed ID: 15935381
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  • 51. Exploiting the right side of the Ramachandran plot: substitution of glycines by D-alanine can significantly increase protein stability.
    Anil B, Song B, Tang Y, Raleigh DP.
    J Am Chem Soc; 2004 Oct 20; 126(41):13194-5. PubMed ID: 15479052
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  • 52.
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  • 53. Water penetration into protein secondary structure revealed by hydrogen-deuterium exchange two-dimensional infrared spectroscopy.
    DeFlores LP, Tokmakoff A.
    J Am Chem Soc; 2006 Dec 27; 128(51):16520-1. PubMed ID: 17177399
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  • 54. Pressure dependence of amide hydrogen-deuterium exchange rates for individual sites in T4 lysozyme.
    Hitchens TK, Bryant RG.
    Biochemistry; 1998 Apr 28; 37(17):5878-87. PubMed ID: 9558321
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  • 56. Engineered symmetric connectivity of secondary structure elements highlights malleability of protein folding pathways.
    Ivarsson Y, Travaglini-Allocatelli C, Brunori M, Gianni S.
    J Am Chem Soc; 2009 Aug 26; 131(33):11727-33. PubMed ID: 19722594
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  • 57. Transition-states in protein folding kinetics: the structural interpretation of Phi values.
    Weikl TR, Dill KA.
    J Mol Biol; 2007 Feb 02; 365(5):1578-86. PubMed ID: 17141267
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  • 58. Different secondary structure elements as scaffolds for protein folding transition states of two homologous four-helix bundles.
    Teilum K, Thormann T, Caterer NR, Poulsen HI, Jensen PH, Knudsen J, Kragelund BB, Poulsen FM.
    Proteins; 2005 Apr 01; 59(1):80-90. PubMed ID: 15690348
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  • 59. Interpretation of p-cyanophenylalanine fluorescence in proteins in terms of solvent exposure and contribution of side-chain quenchers: a combined fluorescence, IR and molecular dynamics study.
    Taskent-Sezgin H, Chung J, Patsalo V, Miyake-Stoner SJ, Miller AM, Brewer SH, Mehl RA, Green DF, Raleigh DP, Carrico I.
    Biochemistry; 2009 Sep 29; 48(38):9040-6. PubMed ID: 19658436
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  • 60. Folding of circular permutants with decreased contact order: general trend balanced by protein stability.
    Lindberg MO, Tångrot J, Otzen DE, Dolgikh DA, Finkelstein AV, Oliveberg M.
    J Mol Biol; 2001 Dec 07; 314(4):891-900. PubMed ID: 11734005
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