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Journal Abstract Search

343 related items for PubMed ID: 24423055

  • 21. 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]

  • 22. Enthalpy of helix-coil transition: missing link in rationalizing the thermodynamics of helix-forming propensities of the amino acid residues.
    Richardson JM, Lopez MM, Makhatadze GI.
    Proc Natl Acad Sci U S A; 2005 Feb 01; 102(5):1413-8. PubMed ID: 15671166
    [Abstract] [Full Text] [Related]

  • 23. Solvation properties of N-substituted cis and trans amides are not identical: significant enthalpy and entropy changes are revealed by the use of variable temperature 1H NMR in aqueous and chloroform solutions and ab initio calculations.
    Troganis AN, Sicilia E, Barbarossou K, Gerothanassis IP, Russo N.
    J Phys Chem A; 2005 Dec 29; 109(51):11878-84. PubMed ID: 16366639
    [Abstract] [Full Text] [Related]

  • 24. Influence of side chain conformations on local conformational features of amino acids and implication for force field development.
    Jiang F, Han W, Wu YD.
    J Phys Chem B; 2010 May 06; 114(17):5840-50. PubMed ID: 20392111
    [Abstract] [Full Text] [Related]

  • 25. Thermodynamics of engineered gold binding peptides: establishing the structure-activity relationships.
    Seker UO, Wilson B, Kulp JL, Evans JS, Tamerler C, Sarikaya M.
    Biomacromolecules; 2014 Jul 14; 15(7):2369-77. PubMed ID: 24892212
    [Abstract] [Full Text] [Related]

  • 26. The conformational manifold of ferricytochrome c explored by visible and far-UV electronic circular dichroism spectroscopy.
    Hagarman A, Duitch L, Schweitzer-Stenner R.
    Biochemistry; 2008 Sep 09; 47(36):9667-77. PubMed ID: 18702508
    [Abstract] [Full Text] [Related]

  • 27. Solvent-exposed residues located in the beta-sheet modulate the stability of the tetramerization domain of p53--a structural and combinatorial approach.
    Mora P, Carbajo RJ, Pineda-Lucena A, Sánchez del Pino MM, Pérez-Payá E.
    Proteins; 2008 Jun 09; 71(4):1670-85. PubMed ID: 18076077
    [Abstract] [Full Text] [Related]

  • 28. Anticooperative Nearest-Neighbor Interactions between Residues in Unfolded Peptides and Proteins.
    Schweitzer-Stenner R, Toal SE.
    Biophys J; 2018 Mar 13; 114(5):1046-1057. PubMed ID: 29539392
    [Abstract] [Full Text] [Related]

  • 29. Alpha-helix stabilization by alanine relative to glycine: roles of polar and apolar solvent exposures and of backbone entropy.
    López-Llano J, Campos LA, Sancho J.
    Proteins; 2006 Aug 15; 64(3):769-78. PubMed ID: 16755589
    [Abstract] [Full Text] [Related]

  • 30. Residual dipolar couplings in short peptides reveal systematic conformational preferences of individual amino acids.
    Dames SA, Aregger R, Vajpai N, Bernado P, Blackledge M, Grzesiek S.
    J Am Chem Soc; 2006 Oct 18; 128(41):13508-14. PubMed ID: 17031964
    [Abstract] [Full Text] [Related]

  • 31. A molecular thermodynamic approach to predict the secondary structure of homopolypeptides in aqueous systems.
    Chen CC, Zhu Y, King JA, Evans LB.
    Biopolymers; 1992 Oct 18; 32(10):1375-92. PubMed ID: 1420965
    [Abstract] [Full Text] [Related]

  • 32. Sensitivity of local hydration behaviour and conformational preferences of peptides to choice of water model.
    Nayar D, Chakravarty C.
    Phys Chem Chem Phys; 2014 Jun 07; 16(21):10199-213. PubMed ID: 24695799
    [Abstract] [Full Text] [Related]

  • 33. Modulation of intrinsic phi,psi propensities of amino acids by neighbouring residues in the coil regions of protein structures: NMR analysis and dissection of a beta-hairpin peptide.
    Griffiths-Jones SR, Sharman GJ, Maynard AJ, Searle MS.
    J Mol Biol; 1998 Dec 18; 284(5):1597-609. PubMed ID: 9878373
    [Abstract] [Full Text] [Related]

  • 34. Origin of the sequence-dependent polyproline II structure in unfolded peptides.
    Kentsis A, Mezei M, Osman R.
    Proteins; 2005 Dec 01; 61(4):769-76. PubMed ID: 16193481
    [Abstract] [Full Text] [Related]

  • 35. Side-chain entropy effects on protein secondary structure formation.
    Chellgren BW, Creamer TP.
    Proteins; 2006 Feb 01; 62(2):411-20. PubMed ID: 16315271
    [Abstract] [Full Text] [Related]

  • 36. 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]

  • 37. Interactions between a helical residue and tertiary structures: helix propensities in small peptides and in native proteins.
    Qian H, Chan SI.
    J Mol Biol; 1996 Aug 16; 261(2):279-88. PubMed ID: 8757294
    [Abstract] [Full Text] [Related]

  • 38. Position dependence of non-polar amino acid intrinsic helical propensities.
    Petukhov M, Muñoz V, Yumoto N, Yoshikawa S, Serrano L.
    J Mol Biol; 1998 Apr 24; 278(1):279-89. PubMed ID: 9571050
    [Abstract] [Full Text] [Related]

  • 39. Comparison between the phi distribution of the amino acids in the protein database and NMR data indicates that amino acids have various phi propensities in the random coil conformation.
    Serrano L.
    J Mol Biol; 1995 Nov 24; 254(2):322-33. PubMed ID: 7490751
    [Abstract] [Full Text] [Related]

  • 40. Amino acids with hydrogen-bonding side chains have an intrinsic tendency to sample various turn conformations in aqueous solution.
    Hagarman A, Mathieu D, Toal S, Measey TJ, Schwalbe H, Schweitzer-Stenner R.
    Chemistry; 2011 Jun 06; 17(24):6789-97. PubMed ID: 21547966
    [Abstract] [Full Text] [Related]

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