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310 related items for PubMed ID: 18713857

  • 1. 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
    [Abstract] [Full Text] [Related]

  • 2. 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]

  • 3. 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 24; 29(7):271-80. PubMed ID: 27284086
    [Abstract] [Full Text] [Related]

  • 4. 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]

  • 5. Intrinsic propensities of amino acid residues in GxG peptides inferred from amide I' band profiles and NMR scalar coupling constants.
    Hagarman A, Measey TJ, Mathieu D, Schwalbe H, Schweitzer-Stenner R.
    J Am Chem Soc; 2010 Jan 20; 132(2):540-51. PubMed ID: 20014772
    [Abstract] [Full Text] [Related]

  • 6. 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]

  • 7. Nature versus design: the conformational propensities of D-amino acids and the importance of side chain chirality.
    Towse CL, Hopping G, Vulovic I, Daggett V.
    Protein Eng Des Sel; 2014 Nov 06; 27(11):447-55. PubMed ID: 25233851
    [Abstract] [Full Text] [Related]

  • 8. The intrinsic conformational features of amino acids from a protein coil library and their applications in force field development.
    Jiang F, Han W, Wu YD.
    Phys Chem Chem Phys; 2013 Mar 14; 15(10):3413-28. PubMed ID: 23385383
    [Abstract] [Full Text] [Related]

  • 9. Experimental verification of force fields for molecular dynamics simulations using Gly-Pro-Gly-Gly.
    Aliev AE, Courtier-Murias D.
    J Phys Chem B; 2010 Sep 30; 114(38):12358-75. PubMed ID: 20825228
    [Abstract] [Full Text] [Related]

  • 10. Insights into Unfolded Proteins from the Intrinsic ϕ/ψ Propensities of the AAXAA Host-Guest Series.
    Towse CL, Vymetal J, Vondrasek J, Daggett V.
    Biophys J; 2016 Jan 19; 110(2):348-361. PubMed ID: 26789758
    [Abstract] [Full Text] [Related]

  • 11. The solution conformations of amino acids from molecular dynamics simulations of Gly-X-Gly peptides: comparison with NMR parameters.
    van der Spoel D.
    Biochem Cell Biol; 1998 Jan 19; 76(2-3):164-70. PubMed ID: 9923685
    [Abstract] [Full Text] [Related]

  • 12. Sparsely populated residue conformations in protein structures: revisiting "experimental" Ramachandran maps.
    Kalmankar NV, Ramakrishnan C, Balaram P.
    Proteins; 2014 Jul 19; 82(7):1101-12. PubMed ID: 23934782
    [Abstract] [Full Text] [Related]

  • 13. 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
    [Abstract] [Full Text] [Related]

  • 14. 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 03; 2(7):596-603. PubMed ID: 7664128
    [Abstract] [Full Text] [Related]

  • 15. Intrinsic secondary structure propensities of the amino acids, using statistical phi-psi matrices: comparison with experimental scales.
    Muñoz V, Serrano L.
    Proteins; 1994 Dec 03; 20(4):301-11. PubMed ID: 7731949
    [Abstract] [Full Text] [Related]

  • 16. Conformational propensities and residual structures in unfolded peptides and proteins.
    Schweitzer-Stenner R.
    Mol Biosyst; 2012 Jan 03; 8(1):122-33. PubMed ID: 21879108
    [Abstract] [Full Text] [Related]

  • 17. 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
    [Abstract] [Full Text] [Related]

  • 18. Role of backbone solvation and electrostatics in generating preferred peptide backbone conformations: distributions of phi.
    Avbelj F, Baldwin RL.
    Proc Natl Acad Sci U S A; 2003 May 13; 100(10):5742-7. PubMed ID: 12709596
    [Abstract] [Full Text] [Related]

  • 19. Local Backbone Geometry Plays a Critical Role in Determining Conformational Preferences of Amino Acid Residues in Proteins.
    Balasco N, Esposito L, De Simone A, Vitagliano L.
    Biomolecules; 2022 Aug 26; 12(9):. PubMed ID: 36139023
    [Abstract] [Full Text] [Related]

  • 20. Structural basis for the varying propensities of different amino acids to adopt the collagen conformation.
    Raman SS, Gopalakrishnan R, Wade RC, Subramanian V.
    J Phys Chem B; 2011 Mar 24; 115(11):2593-607. PubMed ID: 21361324
    [Abstract] [Full Text] [Related]

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