pH-Independence of trialanine and the effects of termini blocking in short peptides: a combined vibrational, NMR, UVCD, and molecular dynamics study S Toal, D Meral, D Verbaro, B Urbanc, R Schweitzer-Stenner The Journal of Physical Chemistry B 117 (14), 3689-3706, 2013 | 77 | 2013 |
Local order in the unfolded state: conformational biases and nearest neighbor interactions S Toal, R Schweitzer-Stenner Biomolecules 4 (3), 725-773, 2014 | 64 | 2014 |
Amino acids with hydrogen‐bonding side chains have an intrinsic tendency to sample various turn conformations in aqueous solution A Hagarman, D Mathieu, S Toal, TJ Measey, H Schwalbe, ... Chemistry–A European Journal 17 (24), 6789-6797, 2011 | 56 | 2011 |
Assessing backbone solvation effects in the conformational propensities of amino acid residues in unfolded peptides NV Ilawe, AE Raeber, R Schweitzer-Stenner, SE Toal, BM Wong Physical Chemistry Chemical Physics 17 (38), 24917-24924, 2015 | 44 | 2015 |
Role of Enthalpy–Entropy Compensation Interactions in Determining the Conformational Propensities of Amino Acid Residues in Unfolded Peptides. SE Toal, DJ Verbaro, R Schweitzer-Stenner The Journal of Physical Chemistry B 118 (5), 1309-1318, 2014 | 44 | 2014 |
Water-Centered Interpretation of Intrinsic pPII Propensities of Amino Acid Residues: In Vitro-Driven Molecular Dynamics Study D Meral, S Toal, R Schweitzer-Stenner, B Urbanc The Journal of Physical Chemistry B 119 (42), 13237-13251, 2015 | 41 | 2015 |
Disorder and order in unfolded and disordered peptides and proteins: A view derived from tripeptide conformational analysis. II. Tripeptides with short side chains populating … K Rybka, SE Toal, DJ Verbaro, D Mathieu, H Schwalbe, ... Proteins: Structure, Function, and Bioinformatics 81 (6), 968-983, 2013 | 41 | 2013 |
Conformational changes of trialanine induced by direct interactions between alanine residues and alcohols in binary mixtures of water with glycerol and ethanol S Toal, O Amidi, R Schweitzer-Stenner Journal of the American Chemical Society 133 (32), 12728-12739, 2011 | 39 | 2011 |
Disorder and order in unfolded and disordered peptides and proteins: a view derived from tripeptide conformational analysis. I. Tripeptides with long and predominantly … R Schweitzer‐Stenner, A Hagarman, S Toal, D Mathieu, H Schwalbe Proteins: Structure, Function, and Bioinformatics 81 (6), 955-967, 2013 | 38 | 2013 |
Randomizing the unfolded state of peptides (and proteins) by nearest neighbor interactions between unlike residues SE Toal, N Kubatova, C Richter, V Linhard, H Schwalbe, ... Chemistry–A European Journal 21 (13), 5173-5192, 2015 | 36* | 2015 |
Demixing of water and ethanol causes conformational redistribution and gelation of the cationic GAG tripeptide B Milorey, S Farrell, SE Toal, R Schweitzer-Stenner Chemical communications 51 (92), 16498-16501, 2015 | 35 | 2015 |
Triaspartate: a model system for conformationally flexible DDD motifs in proteins L Duitch, S Toal, TJ Measey, R Schweitzer-Stenner The Journal of Physical Chemistry B 116 (17), 5160-5171, 2012 | 23 | 2012 |
Construction and comparison of the statistical coil states of unfolded and intrinsically disordered proteins from nearest-neighbor corrected conformational propensities of … R Schweitzer-Stenner, SE Toal Molecular BioSystems 12 (11), 3294-3306, 2016 | 19 | 2016 |
Water-mediated electronic structure of oligopeptides probed by their UV circular dichroism, absorption spectra, and time-dependent DFT calculations A Kumar, SE Toal, D DiGuiseppi, R Schweitzer-Stenner, BM Wong The Journal of Physical Chemistry B 124 (13), 2579-2590, 2020 | 17 | 2020 |
Ionized Trilysine: A Model System for Understanding the Nonrandom Structure of Poly-l-lysine and Lysine-Containing Motifs in Proteins DJ Verbaro, D Mathieu, SE Toal, H Schwalbe, R Schweitzer-Stenner The Journal of Physical Chemistry B 116 (28), 8084-8094, 2012 | 17 | 2012 |
Anticooperative nearest-neighbor interactions between residues in unfolded peptides and proteins R Schweitzer-Stenner, SE Toal Biophysical Journal 114 (5), 1046-1057, 2018 | 16 | 2018 |
Entropy reduction in unfolded peptides (and proteins) due to conformational preferences of amino acid residues R Schweitzer-Stenner, SE Toal Physical Chemistry Chemical Physics 16 (41), 22527-22536, 2014 | 15 | 2014 |
Investigating the formation of a repulsive hydrogel of a cationic 16mer peptide at low ionic strength in water by vibrational spectroscopy and rheology D DiGuiseppi, J Kraus, SE Toal, N Alvarez, R Schweitzer-Stenner The Journal of Physical Chemistry B 120 (38), 10079-10090, 2016 | 10 | 2016 |
Structural analysis of unfolded peptides by Raman spectroscopy R Schweitzer-Stenner, JB Soffer, S Toal, D Verbaro Intrinsically Disordered Protein Analysis: Volume 1, Methods and …, 2012 | 7 | 2012 |
The TrpA protein of Trichodesmium erythraeum IMS101 is a non-fibril-forming collagen and a component of the outer sheath S Price, S Toal, S Anandan Microbiology 160 (10), 2148-2156, 2014 | 6 | 2014 |