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Siobhan E. Toal, Ph.D. - Publications

Affiliations: 
2014 Chemistry (College of Arts and Sciences) Drexel University, Philadelphia, PA, United States 
Area:
Polymer Chemistry, General Biophysics
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34 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2020 Kumar A, Toal SE, DiGuiseppi D, Schweitzer-Stenner R, Wong BM. Water-Mediated Electronic Structure of Oligopeptides Probed by Their UV Circular Dichroism, Absorption Spectra, and Time-Dependent DFT Calculations. The Journal of Physical Chemistry. B. PMID 32207305 DOI: 10.1021/Acs.Jpcb.0C00657  0.762
2018 Schweitzer-Stenner R, Toal SE. Anticooperative Nearest-Neighbor Interactions between Residues in Unfolded Peptides and Proteins. Biophysical Journal. 114: 1046-1057. PMID 29539392 DOI: 10.1016/J.Bpj.2018.01.022  0.727
2018 Schweitzer-Stenner R, Toal SE. Anti-cooperative Nearest Neighbor Coupling Determines the Statistical Coil State of Peptides and Proteins at High Temperatures Biophysical Journal. 114: 588a. DOI: 10.1016/J.Bpj.2017.11.3217  0.661
2017 Toal SE, Kubatova N, Richter C, Linhard V, Schwalbe H, Schweitzer-Stenner R. Chemistry (Weinheim An Der Bergstrasse, Germany). 23: 18084-18087. PMID 29265638 DOI: 10.1186/1742-4690-3-S1-S58  0.627
2017 Toal S, Trexler A, DeWitt D, Brown M, Rhoades E. Determining the Role of N-Terminal Acetylation on α-Synuclein Function Biophysical Journal. 112: 366a. DOI: 10.1016/J.Bpj.2016.11.1982  0.307
2016 DiGuiseppi D, Kraus J, Toal SE, Alvarez NJ, Schweitzer-Stenner R. Investigating the Formation of a Repulsive Hydrogel of a Cationic 16mer Peptide at Low Ionic Strength in Water by Vibrational Spectroscopy and Rheology. The Journal of Physical Chemistry. B. PMID 27582028 DOI: 10.1021/Acs.Jpcb.6B07673  0.733
2016 Schweitzer-Stenner R, Toal SE. Construction and comparison of the statistical coil states of unfolded and intrinsically disordered proteins from nearest-neighbor corrected conformational propensities of short peptides. Molecular Biosystems. PMID 27545097 DOI: 10.1039/C6Mb00489J  0.722
2016 Toal S, DeWitt D, Trexler A, Brown M, Rhoades E. Assessing N-Terminal Modifications on Alpha-Synuclein Structure and Function Biophysical Journal. 110: 552a. DOI: 10.1016/J.Bpj.2015.11.2954  0.392
2015 Meral D, Toal S, Schweitzer-Stenner R, Urbanc B. Water-Centered Interpretation of Intrinsic pPII Propensities of Amino Acid Residues: In Vitro-Driven Molecular Dynamics Study. The Journal of Physical Chemistry. B. 119: 13237-51. PMID 26418575 DOI: 10.1021/Acs.Jpcb.5B06281  0.696
2015 Milorey B, Farrell S, Toal SE, Schweitzer-Stenner R. Demixing of water and ethanol causes conformational redistribution and gelation of the cationic GAG tripeptide. Chemical Communications (Cambridge, England). 51: 16498-501. PMID 26414527 DOI: 10.1039/C5Cc06097D  0.618
2015 Ilawe NV, Raeber AE, Schweitzer-Stenner R, Toal SE, Wong BM. Assessing backbone solvation effects in the conformational propensities of amino acid residues in unfolded peptides. Physical Chemistry Chemical Physics : Pccp. 17: 24917-24. PMID 26343224 DOI: 10.1039/C5Cp03646A  0.809
2015 Toal SE, Kubatova N, Richter C, Linhard V, Schwalbe H, Schweitzer-Stenner R. Randomizing the unfolded state of peptides (and proteins) by nearest neighbor interactions between unlike residues. Chemistry (Weinheim An Der Bergstrasse, Germany). 21: 5173-92. PMID 25728043 DOI: 10.1002/Chem.201406539  0.782
2015 Milorey B, Farrell S, Toal SE, Schweitzer-Stenner R. Conformational Effects on Alanine Induced Induced by Various Alcohol Cosolvents Biophysical Journal. 108: 230a. DOI: 10.1016/J.Bpj.2014.11.1271  0.69
2015 Toal S, Richter C, Kubatova N, Schwalbe H, Schweitzer-Stenner R. Randomizing Intrinsic Conformational Biases by Nearest Neighbor Interactions between Unlike Residues Biophysical Journal. 108: 230a. DOI: 10.1016/J.Bpj.2014.11.1270  0.754
2015 Schweitzer-Stenner R, Toal SE. Conformational Entropies of Unfolded Peptides: The Source of a Realistic Estimation of the Entropy of Unfolded Peptides and Proteins Biophysical Journal. 108: 194a. DOI: 10.1016/J.Bpj.2014.11.1073  0.762
2014 Schweitzer-Stenner R, Toal SE. Entropy reduction in unfolded peptides (and proteins) due to conformational preferences of amino acid residues. Physical Chemistry Chemical Physics : Pccp. 16: 22527-36. PMID 25227444 DOI: 10.1039/C4Cp02108H  0.745
2014 Toal S, Schweitzer-Stenner R. Local order in the unfolded state: conformational biases and nearest neighbor interactions. Biomolecules. 4: 725-73. PMID 25062017 DOI: 10.3390/biom4030725  0.729
2014 Price S, Toal S, Anandan S. The TrpA protein of Trichodesmium erythraeum IMS101 is a non-fibril-forming collagen and a component of the outer sheath. Microbiology (Reading, England). 160: 2148-56. PMID 25009239 DOI: 10.1099/Mic.0.079475-0  0.361
2014 Toal SE, Verbaro DJ, Schweitzer-Stenner R. Role of enthalpy-entropy compensation interactions in determining the conformational propensities of amino acid residues in unfolded peptides. The Journal of Physical Chemistry. B. 118: 1309-18. PMID 24423055 DOI: 10.1021/Jp500181D  0.735
2014 Toal S, Schweitzer-Stenner R, Rybka K, Schwalbe H. Nearest Neighbor Interactions Attenuate Intrinsic Amino Acid Conformational Preferences: A Combined Vibrational and NMR Study Biophysical Journal. 106: 689a. DOI: 10.1016/J.Bpj.2013.11.3811  0.751
2014 Toal S, Verbaro D, Schweitzer-Stenner R. Enthalpy-Entropy Compensation and Isoequilbria Implicate Solvation as the Driving Force for Amino Acid Conformational Propensity Biophysical Journal. 106: 689a. DOI: 10.1016/J.Bpj.2013.11.3810  0.751
2013 Toal S, Meral D, Verbaro D, Urbanc B, Schweitzer-Stenner R. pH-Independence of trialanine and the effects of termini blocking in short peptides: a combined vibrational, NMR, UVCD, and molecular dynamics study. The Journal of Physical Chemistry. B. 117: 3689-706. PMID 23448349 DOI: 10.1021/Jp310466B  0.778
2013 Rybka K, Toal SE, Verbaro DJ, Mathieu D, Schwalbe H, Schweitzer-Stenner R. 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. Proteins. 81: 968-83. PMID 23229867 DOI: 10.1002/Prot.24226  0.769
2013 Schweitzer-Stenner R, Hagarman A, Toal S, Mathieu D, Schwalbe H. 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. Proteins. 81: 955-67. PMID 23229832 DOI: 10.1002/Prot.24225  0.826
2013 Toal S, Schweitzer-Stenner R, Rybka K, Schwalbe H. How do Nearest-Neighbor Interactions Effect the Conformational Distributions in Peptides? Biophysical Journal. 104: 55a. DOI: 10.1016/J.Bpj.2012.11.345  0.774
2013 Sasimovich I, Measey T, Toal S, Schweitzer-Stenner R, Decatur S. Investigating the Self-Aggregation of a Polyalanine Peptide: Kinetics and Isotope Edited Studies Biophysical Journal. 104: 54a. DOI: 10.1016/J.Bpj.2012.11.341  0.816
2012 Schweitzer-Stenner R, Soffer JB, Toal S, Verbaro D. Structural analysis of unfolded peptides by Raman spectroscopy. Methods in Molecular Biology (Clifton, N.J.). 895: 315-46. PMID 22760326 DOI: 10.1007/978-1-61779-927-3_19  0.81
2012 Verbaro DJ, Mathieu D, Toal SE, Schwalbe H, Schweitzer-Stenner R. Ionized trilysine: a model system for understanding the nonrandom structure of poly-L-lysine and lysine-containing motifs in proteins. The Journal of Physical Chemistry. B. 116: 8084-94. PMID 22712805 DOI: 10.1021/Jp303794S  0.787
2012 Duitch L, Toal S, Measey TJ, Schweitzer-Stenner R. Triaspartate: a model system for conformationally flexible DDD motifs in proteins. The Journal of Physical Chemistry. B. 116: 5160-71. PMID 22435395 DOI: 10.1021/Jp2121565  0.84
2011 Toal S, Amidi O, Schweitzer-Stenner R. Conformational changes of trialanine induced by direct interactions between alanine residues and alcohols in binary mixtures of water with glycerol and ethanol. Journal of the American Chemical Society. 133: 12728-39. PMID 21728315 DOI: 10.1021/Ja204123G  0.69
2011 Hagarman A, Mathieu D, Toal S, Measey TJ, Schwalbe H, Schweitzer-Stenner R. Amino acids with hydrogen-bonding side chains have an intrinsic tendency to sample various turn conformations in aqueous solution. Chemistry (Weinheim An Der Bergstrasse, Germany). 17: 6789-97. PMID 21547966 DOI: 10.1002/Chem.201100016  0.798
2011 Toal S, Amidi O, Schweitzer-Stenner R. Solvent Dependence of Trialanine Conformers Biophysical Journal. 100: 62a. DOI: 10.1016/J.Bpj.2010.12.539  0.712
2011 Duitch L, Toal S, Verbaro D, Hagarman A, Schweitzer-Stenner R. Tri-Aspartic Acid Peptides in Water: A Suitable Model System for Determining the Structural Propensities of DxD Motifs in Unfolded Proteins Biophysical Journal. 100: 61a. DOI: 10.1016/J.Bpj.2010.12.533  0.804
2011 Schweitzer-Stenner R, Toal S, Measey TJ. The Utilization of the Anomalous Intensity Enhancement of the Amide I Couplet for Probing the Formation of Peptide Fibrils in Solution Biophysical Journal. 100: 14a. DOI: 10.1016/J.Bpj.2010.12.285  0.783
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