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176 related items for PubMed ID: 35625612

  • 1. 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]

  • 2. 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]

  • 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. 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]

  • 5. Conformational propensities and residual structures in unfolded peptides and proteins.
    Schweitzer-Stenner R.
    Mol Biosyst; 2012 Jan 13; 8(1):122-33. PubMed ID: 21879108
    [Abstract] [Full Text] [Related]

  • 6. 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]

  • 7. 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]

  • 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. 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. 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]

  • 11. 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]

  • 12. 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]

  • 13. 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 14; 81(6):955-67. PubMed ID: 23229832
    [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. 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]

  • 16. 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]

  • 17. The relevance of short peptides for an understanding of unfolded and intrinsically disordered proteins.
    Schweitzer-Stenner R.
    Phys Chem Chem Phys; 2023 May 03; 25(17):11908-11933. PubMed ID: 37096579
    [Abstract] [Full Text] [Related]

  • 18. 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]

  • 19. Short peptides as predictors for the structure of polyarginine sequences in disordered proteins.
    Milorey B, Schweitzer-Stenner R, Andrews B, Schwalbe H, Urbanc B.
    Biophys J; 2021 Feb 16; 120(4):662-676. PubMed ID: 33453267
    [Abstract] [Full Text] [Related]

  • 20. 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]

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