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Journal Abstract Search

305 related items for PubMed ID: 25062017

  • 1. 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]

  • 2. 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]

  • 3. Conformational propensities and residual structures in unfolded peptides and proteins.
    Schweitzer-Stenner R.
    Mol Biosyst; 2012 Jan 18; 8(1):122-33. PubMed ID: 21879108
    [Abstract] [Full Text] [Related]

  • 4. 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]

  • 5. 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]

  • 6. Exploring Nearest Neighbor Interactions and Their Influence on the Gibbs Energy Landscape of Unfolded Proteins and Peptides.
    Schweitzer-Stenner R.
    Int J Mol Sci; 2022 May 18; 23(10):. PubMed ID: 35628453
    [Abstract] [Full Text] [Related]

  • 7. 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]

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  • 9. Helix, sheet, and polyproline II frequencies and strong nearest neighbor effects in a restricted coil library.
    Jha AK, Colubri A, Zaman MH, Koide S, Sosnick TR, Freed KF.
    Biochemistry; 2005 Jul 19; 44(28):9691-702. PubMed ID: 16008354
    [Abstract] [Full Text] [Related]

  • 10. 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]

  • 11. 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]

  • 12. 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]

  • 13. Entropy reduction in unfolded peptides (and proteins) due to conformational preferences of amino acid residues.
    Schweitzer-Stenner R, Toal SE.
    Phys Chem Chem Phys; 2014 Nov 07; 16(41):22527-36. PubMed ID: 25227444
    [Abstract] [Full Text] [Related]

  • 14. 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]

  • 15. 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]

  • 16. A simple model for polyproline II structure in unfolded states of alanine-based peptides.
    Pappu RV, Rose GD.
    Protein Sci; 2002 Oct 13; 11(10):2437-55. PubMed ID: 12237465
    [Abstract] [Full Text] [Related]

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

  • 18. Conformational propensities of protein folding intermediates: distribution of species in the 1S, 2S, and 3S ensembles of the [C40A,C95A] mutant of bovine pancreatic ribonuclease A.
    Wedemeyer WJ, Xu X, Welker E, Scheraga HA.
    Biochemistry; 2002 Feb 05; 41(5):1483-91. PubMed ID: 11814341
    [Abstract] [Full Text] [Related]

  • 19. Unfolded protein ensembles, folding trajectories, and refolding rate prediction.
    Das A, Sin BK, Mohazab AR, Plotkin SS.
    J Chem Phys; 2013 Sep 28; 139(12):121925. PubMed ID: 24089737
    [Abstract] [Full Text] [Related]

  • 20. Conformational propensities of intrinsically disordered proteins from NMR chemical shifts.
    Kragelj J, Ozenne V, Blackledge M, Jensen MR.
    Chemphyschem; 2013 Sep 16; 14(13):3034-45. PubMed ID: 23794453
    [Abstract] [Full Text] [Related]

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