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Journal Abstract Search

136 related items for PubMed ID: 34619031

  • 1.
    ; . PubMed ID:
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  • 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. 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]

  • 4. Conformational propensities and residual structures in unfolded peptides and proteins.
    Schweitzer-Stenner R.
    Mol Biosyst; 2012 Jan 23; 8(1):122-33. PubMed ID: 21879108
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  • 5. Amino acids with hydrogen-bonding side chains have an intrinsic tendency to sample various turn conformations in aqueous solution.
    Hagarman A, Mathieu D, Toal S, Measey TJ, Schwalbe H, Schweitzer-Stenner R.
    Chemistry; 2011 Jun 06; 17(24):6789-97. PubMed ID: 21547966
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  • 6. 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]

  • 7. 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]

  • 8. 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]

  • 9. 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]

  • 10. 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]

  • 11. 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]

  • 12. 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 16; 81(6):968-83. PubMed ID: 23229867
    [Abstract] [Full Text] [Related]

  • 13.
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  • 14. 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]

  • 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. NMR structural and dynamic characterization of the acid-unfolded state of apomyoglobin provides insights into the early events in protein folding.
    Yao J, Chung J, Eliezer D, Wright PE, Dyson HJ.
    Biochemistry; 2001 Mar 27; 40(12):3561-71. PubMed ID: 11297422
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  • 17.
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  • 19. 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]

  • 20. 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]

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