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Journal Abstract Search

208 related items for PubMed ID: 10430897

  • 1. Intrinsic beta-sheet propensities result from van der Waals interactions between side chains and the local backbone.
    Street AG, Mayo SL.
    Proc Natl Acad Sci U S A; 1999 Aug 03; 96(16):9074-6. PubMed ID: 10430897
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  • 3. Amino acid conformational preferences and solvation of polar backbone atoms in peptides and proteins.
    Avbelj F.
    J Mol Biol; 2000 Jul 28; 300(5):1335-59. PubMed ID: 10903873
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  • 5. The intrinsic conformational propensities of the 20 naturally occurring amino acids and reflection of these propensities in proteins.
    Beck DA, Alonso DO, Inoyama D, Daggett V.
    Proc Natl Acad Sci U S A; 2008 Aug 26; 105(34):12259-64. PubMed ID: 18713857
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  • 6. The effect of chirality and steric hindrance on intrinsic backbone conformational propensities: tools for protein design.
    Childers MC, Towse CL, Daggett V.
    Protein Eng Des Sel; 2016 Jul 26; 29(7):271-80. PubMed ID: 27284086
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  • 8. 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
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  • 9. Measurement of the beta-sheet-forming propensities of amino acids.
    Minor DL, Kim PS.
    Nature; 1994 Feb 17; 367(6464):660-3. PubMed ID: 8107853
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  • 10. Intrinsic secondary structure propensities of the amino acids, using statistical phi-psi matrices: comparison with experimental scales.
    Muñoz V, Serrano L.
    Proteins; 1994 Dec 17; 20(4):301-11. PubMed ID: 7731949
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  • 11. beta-sheet propensity and its correlation with parameters based on conformation.
    Pal D, Chakrabarti P.
    Acta Crystallogr D Biol Crystallogr; 2000 May 17; 56(Pt 5):589-94. PubMed ID: 10771428
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  • 12. 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
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  • 13. Side-chain entropy opposes alpha-helix formation but rationalizes experimentally determined helix-forming propensities.
    Creamer TP, Rose GD.
    Proc Natl Acad Sci U S A; 1992 Jul 01; 89(13):5937-41. PubMed ID: 1631077
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  • 16. Intrinsic phi, psi propensities of amino acids, derived from the coil regions of known structures.
    Swindells MB, MacArthur MW, Thornton JM.
    Nat Struct Biol; 1995 Jul 01; 2(7):596-603. PubMed ID: 7664128
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  • 17. Solvation thermodynamics of amino acid side chains on a short peptide backbone.
    Hajari T, van der Vegt NF.
    J Chem Phys; 2015 Apr 14; 142(14):144502. PubMed ID: 25877585
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  • 19. Evidence for strained interactions between side-chains and the polypeptide backbone.
    Stites WE, Meeker AK, Shortle D.
    J Mol Biol; 1994 Jan 07; 235(1):27-32. PubMed ID: 8289248
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  • 20. Periodicity of polar and nonpolar amino acids is the major determinant of secondary structure in self-assembling oligomeric peptides.
    Xiong H, Buckwalter BL, Shieh HM, Hecht MH.
    Proc Natl Acad Sci U S A; 1995 Jul 03; 92(14):6349-53. PubMed ID: 7603994
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