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194 related items for PubMed ID: 33453267

  • 1. 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]

  • 2. 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]

  • 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. Do molecular dynamics force fields accurately model Ramachandran distributions of amino acid residues in water?
    Andrews B, Guerra J, Schweitzer-Stenner R, Urbanc B.
    Phys Chem Chem Phys; 2022 Feb 02; 24(5):3259-3279. PubMed ID: 35048087
    [Abstract] [Full Text] [Related]

  • 5. Discrepancies between conformational distributions of a polyalanine peptide in solution obtained from molecular dynamics force fields and amide I' band profiles.
    Verbaro D, Ghosh I, Nau WM, Schweitzer-Stenner R.
    J Phys Chem B; 2010 Dec 30; 114(51):17201-8. PubMed ID: 21138254
    [Abstract] [Full Text] [Related]

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  • 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. 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]

  • 9. Hydrodynamic Radii of Intrinsically Disordered Proteins Determined from Experimental Polyproline II Propensities.
    Tomasso ME, Tarver MJ, Devarajan D, Whitten ST.
    PLoS Comput Biol; 2016 Jan 19; 12(1):e1004686. PubMed ID: 26727467
    [Abstract] [Full Text] [Related]

  • 10. 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]

  • 11. 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]

  • 12. 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]

  • 13. 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]

  • 14. 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]

  • 15. 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]

  • 16. Conformational propensities and residual structures in unfolded peptides and proteins.
    Schweitzer-Stenner R.
    Mol Biosyst; 2012 Jan 26; 8(1):122-33. PubMed ID: 21879108
    [Abstract] [Full Text] [Related]

  • 17. Conformational Preferences of an Intrinsically Disordered Protein Domain: A Case Study for Modern Force Fields.
    Gopal SM, Wingbermühle S, Schnatwinkel J, Juber S, Herrmann C, Schäfer LV.
    J Phys Chem B; 2021 Jan 14; 125(1):24-35. PubMed ID: 33382616
    [Abstract] [Full Text] [Related]

  • 18. Distribution of conformations sampled by the central amino acid residue in tripeptides inferred from amide I band profiles and NMR scalar coupling constants.
    Schweitzer-Stenner R.
    J Phys Chem B; 2009 Mar 05; 113(9):2922-32. PubMed ID: 19243204
    [Abstract] [Full Text] [Related]

  • 19. Macromolecular crowding: chemistry and physics meet biology (Ascona, Switzerland, 10-14 June 2012).
    Foffi G, Pastore A, Piazza F, Temussi PA.
    Phys Biol; 2013 Aug 05; 10(4):040301. PubMed ID: 23912807
    [Abstract] [Full Text] [Related]

  • 20. Molecular Dynamics Simulations of Phosphorylated Intrinsically Disordered Proteins: A Force Field Comparison.
    Rieloff E, Skepö M.
    Int J Mol Sci; 2021 Sep 21; 22(18):. PubMed ID: 34576338
    [Abstract] [Full Text] [Related]

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