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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