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Journal Abstract Search

139 related items for PubMed ID: 25728043

  • 1. Randomizing the unfolded state of peptides (and proteins) by nearest neighbor interactions between unlike residues.
    Toal SE, Kubatova N, Richter C, Linhard V, Schwalbe H, Schweitzer-Stenner R.
    Chemistry; 2015 Mar 23; 21(13):5173-92. PubMed ID: 25728043
    [Abstract] [Full Text] [Related]

  • 2. Triaspartate: a model system for conformationally flexible DDD motifs in proteins.
    Duitch L, Toal S, Measey TJ, Schweitzer-Stenner R.
    J Phys Chem B; 2012 May 03; 116(17):5160-71. PubMed ID: 22435395
    [Abstract] [Full Text] [Related]

  • 3. Construction and comparison of the statistical coil states of unfolded and intrinsically disordered proteins from nearest-neighbor corrected conformational propensities of short peptides.
    Schweitzer-Stenner R, Toal SE.
    Mol Biosyst; 2016 Oct 18; 12(11):3294-3306. PubMed ID: 27545097
    [Abstract] [Full Text] [Related]

  • 4. Ionized trilysine: a model system for understanding the nonrandom structure of poly-L-lysine and lysine-containing motifs in proteins.
    Verbaro DJ, Mathieu D, Toal SE, Schwalbe H, Schweitzer-Stenner R.
    J Phys Chem B; 2012 Jul 19; 116(28):8084-94. PubMed ID: 22712805
    [Abstract] [Full Text] [Related]

  • 5. Conformational changes of trialanine induced by direct interactions between alanine residues and alcohols in binary mixtures of water with glycerol and ethanol.
    Toal S, Amidi O, Schweitzer-Stenner R.
    J Am Chem Soc; 2011 Aug 17; 133(32):12728-39. PubMed ID: 21728315
    [Abstract] [Full Text] [Related]

  • 6. Role of enthalpy-entropy compensation interactions in determining the conformational propensities of amino acid residues in unfolded peptides.
    Toal SE, Verbaro DJ, Schweitzer-Stenner R.
    J Phys Chem B; 2014 Feb 06; 118(5):1309-18. PubMed ID: 24423055
    [Abstract] [Full Text] [Related]

  • 7. pH-Independence of trialanine and the effects of termini blocking in short peptides: a combined vibrational, NMR, UVCD, and molecular dynamics study.
    Toal S, Meral D, Verbaro D, Urbanc B, Schweitzer-Stenner R.
    J Phys Chem B; 2013 Apr 11; 117(14):3689-706. PubMed ID: 23448349
    [Abstract] [Full Text] [Related]

  • 8. 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]

  • 9. 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]

  • 10. Randomizing of Oligopeptide Conformations by Nearest Neighbor Interactions between Amino Acid Residues.
    Schweitzer-Stenner R, Milorey B, Schwalbe H.
    Biomolecules; 2022 May 11; 12(5):. PubMed ID: 35625612
    [Abstract] [Full Text] [Related]

  • 11. Repeating Aspartic Acid Residues Prefer Turn-like Conformations in the Unfolded State: Implications for Early Protein Folding.
    Milorey B, Schwalbe H, O'Neill N, Schweitzer-Stenner R.
    J Phys Chem B; 2021 Oct 21; 125(41):11392-11407. PubMed ID: 34619031
    [Abstract] [Full Text] [Related]

  • 12. Neighbor effect on PPII conformation in alanine peptides.
    Chen K, Liu Z, Zhou C, Shi Z, Kallenbach NR.
    J Am Chem Soc; 2005 Jul 27; 127(29):10146-7. PubMed ID: 16028907
    [Abstract] [Full Text] [Related]

  • 13. Water-Centered Interpretation of Intrinsic pPII Propensities of Amino Acid Residues: In Vitro-Driven Molecular Dynamics Study.
    Meral D, Toal S, Schweitzer-Stenner R, Urbanc B.
    J Phys Chem B; 2015 Oct 22; 119(42):13237-51. PubMed ID: 26418575
    [Abstract] [Full Text] [Related]

  • 14. Disorder and order in unfolded and disordered peptides and proteins: a view derived from tripeptide conformational analysis. II. Tripeptides with short side chains populating asx and β-type like turn conformations.
    Rybka K, Toal SE, Verbaro DJ, Mathieu D, Schwalbe H, Schweitzer-Stenner R.
    Proteins; 2013 Jun 22; 81(6):968-83. PubMed ID: 23229867
    [Abstract] [Full Text] [Related]

  • 15. Local order in the unfolded state: conformational biases and nearest neighbor interactions.
    Toal S, Schweitzer-Stenner R.
    Biomolecules; 2014 Jul 24; 4(3):725-73. PubMed ID: 25062017
    [Abstract] [Full Text] [Related]

  • 16. Disorder and order in unfolded and disordered peptides and proteins: a view derived from tripeptide conformational analysis. I. Tripeptides with long and predominantly hydrophobic side chains.
    Schweitzer-Stenner R, Hagarman A, Toal S, Mathieu D, Schwalbe H.
    Proteins; 2013 Jun 24; 81(6):955-67. PubMed ID: 23229832
    [Abstract] [Full Text] [Related]

  • 17. Determinants of the polyproline II helix from modeling studies.
    Creamer TP, Campbell MN.
    Adv Protein Chem; 2002 Jun 24; 62():263-82. PubMed ID: 12418106
    [Abstract] [Full Text] [Related]

  • 18. Assessing backbone solvation effects in the conformational propensities of amino acid residues in unfolded peptides.
    Ilawe NV, Raeber AE, Schweitzer-Stenner R, Toal SE, Wong BM.
    Phys Chem Chem Phys; 2015 Oct 14; 17(38):24917-24. PubMed ID: 26343224
    [Abstract] [Full Text] [Related]

  • 19. Conformational propensities and residual structures in unfolded peptides and proteins.
    Schweitzer-Stenner R.
    Mol Biosyst; 2012 Jan 14; 8(1):122-33. PubMed ID: 21879108
    [Abstract] [Full Text] [Related]

  • 20. The effect of the polyproline II (PPII) conformation on the denatured state entropy.
    Ferreon JC, Hilser VJ.
    Protein Sci; 2003 Mar 14; 12(3):447-57. PubMed ID: 12592015
    [Abstract] [Full Text] [Related]

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