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360 related items for PubMed ID: 27545097

  • 1. 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]

  • 2. 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]

  • 3. 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]

  • 4. 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]

  • 5. 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]

  • 6. Structural and Energetic Characterization of the Denatured State from the Perspectives of Peptides, the Coil Library, and Intrinsically Disordered Proteins.
    Paiz EA, Lewis KA, Whitten ST.
    Molecules; 2021 Jan 26; 26(3):. PubMed ID: 33530506
    [Abstract] [Full Text] [Related]

  • 7. 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]

  • 8. Conformational propensities and residual structures in unfolded peptides and proteins.
    Schweitzer-Stenner R.
    Mol Biosyst; 2012 Jan 24; 8(1):122-33. PubMed ID: 21879108
    [Abstract] [Full Text] [Related]

  • 9. Prediction of nearest neighbor effects on backbone torsion angles and NMR scalar coupling constants in disordered proteins.
    Shen Y, Roche J, Grishaev A, Bax A.
    Protein Sci; 2018 Jan 24; 27(1):146-158. PubMed ID: 28884933
    [Abstract] [Full Text] [Related]

  • 10. The Nearest-Neighbor Effect on Random-Coil NMR Chemical Shifts Demonstrated Using a Low-Complexity Amino-Acid Sequence.
    Chen TC, Hsiao CL, Huang SJ, Huang JR.
    Protein Pept Lett; 2016 Jan 24; 23(11):967-975. PubMed ID: 27653629
    [Abstract] [Full Text] [Related]

  • 11. 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]

  • 12. A J-modulated protonless NMR experiment characterizes the conformational ensemble of the intrinsically disordered protein WIP.
    Rozentur-Shkop E, Goobes G, Chill JH.
    J Biomol NMR; 2016 Dec 03; 66(4):243-257. PubMed ID: 27844185
    [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. 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]

  • 15. 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 03; 81(6):955-67. PubMed ID: 23229832
    [Abstract] [Full Text] [Related]

  • 16. 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]

  • 17. Impact of Heat on Coil Hydrodynamic Size Yields the Energetics of Denatured State Conformational Bias.
    English LR, Voss SM, Tilton EC, Paiz EA, So S, Parra GL, Whitten ST.
    J Phys Chem B; 2019 Nov 27; 123(47):10014-10024. PubMed ID: 31679343
    [Abstract] [Full Text] [Related]

  • 18. Neighboring residue effects in terminally blocked dipeptides: implications for residual secondary structures in intrinsically unfolded/disordered proteins.
    Jung YS, Oh KI, Hwang GS, Cho M.
    Chirality; 2014 Sep 27; 26(9):443-52. PubMed ID: 24453185
    [Abstract] [Full Text] [Related]

  • 19. 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]

  • 20. 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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