Siobhan Toal

648 total citations
21 papers, 575 citations indexed

About

Siobhan Toal is a scholar working on Molecular Biology, Spectroscopy and Atomic and Molecular Physics, and Optics. According to data from OpenAlex, Siobhan Toal has authored 21 papers receiving a total of 575 indexed citations (citations by other indexed papers that have themselves been cited), including 20 papers in Molecular Biology, 11 papers in Spectroscopy and 5 papers in Atomic and Molecular Physics, and Optics. Recurrent topics in Siobhan Toal's work include Protein Structure and Dynamics (16 papers), Chemical Synthesis and Analysis (8 papers) and Molecular spectroscopy and chirality (7 papers). Siobhan Toal is often cited by papers focused on Protein Structure and Dynamics (16 papers), Chemical Synthesis and Analysis (8 papers) and Molecular spectroscopy and chirality (7 papers). Siobhan Toal collaborates with scholars based in United States, Germany and Slovenia. Siobhan Toal's co-authors include Reinhard Schweitzer‐Stenner, Daniel Verbaro, Harald Schwalbe, Daniel Mathieu, Brigita Urbanc, Andrew Hagarman, Thomas J. Measey, Bryan M. Wong, Niranjan V. Ilawe and V.L. Linhard and has published in prestigious journals such as Journal of the American Chemical Society, The Journal of Physical Chemistry B and Chemical Communications.

In The Last Decade

Siobhan Toal

20 papers receiving 574 citations

Peers

Siobhan Toal
Andrew Hagarman United States
Benjamin M. Bulheller United Kingdom
Thomas J. Measey United States
Maik H. Jacob Germany
Wayne R. Fiori United States
Wládia Viviani Brazil
Jeffrey Mills United States
William Shalongo United States
Heiko Schäfer Switzerland
Michelle R. Bunagan United States
Andrew Hagarman United States
Siobhan Toal
Citations per year, relative to Siobhan Toal Siobhan Toal (= 1×) peers Andrew Hagarman

Countries citing papers authored by Siobhan Toal

Since Specialization
Citations

This map shows the geographic impact of Siobhan Toal's research. It shows the number of citations coming from papers published by authors working in each country. You can also color the map by specialization and compare the number of citations received by Siobhan Toal with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites Siobhan Toal more than expected).

Fields of papers citing papers by Siobhan Toal

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Siobhan Toal. Nodes represent research fields, and links connect fields that are likely to share authors. Colored nodes show fields that tend to cite the papers produced by Siobhan Toal. The network helps show where Siobhan Toal may publish in the future.

Co-authorship network of co-authors of Siobhan Toal

This figure shows the co-authorship network connecting the top 25 collaborators of Siobhan Toal. A scholar is included among the top collaborators of Siobhan Toal based on the total number of citations received by their joint publications. Widths of edges represent the number of papers authors have co-authored together. Node borders signify the number of papers an author published with Siobhan Toal. Siobhan Toal is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

20 of 20 papers shown
1.
Toal, Siobhan, et al.. (2020). 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. 124(13). 2579–2590. 18 indexed citations
2.
Schweitzer‐Stenner, Reinhard & Siobhan Toal. (2018). Anticooperative Nearest-Neighbor Interactions between Residues in Unfolded Peptides and Proteins. Biophysical Journal. 114(5). 1046–1057. 13 indexed citations
3.
4.
Kraus, Jodi, et al.. (2016). 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. 120(38). 10079–10090. 11 indexed citations
5.
Toal, Siobhan, et al.. (2015). Water-Centered Interpretation of Intrinsic pPII Propensities of Amino Acid Residues: In Vitro-Driven Molecular Dynamics Study. The Journal of Physical Chemistry B. 119(42). 13237–13251. 35 indexed citations
6.
Ilawe, Niranjan V., et al.. (2015). Assessing backbone solvation effects in the conformational propensities of amino acid residues in unfolded peptides. Physical Chemistry Chemical Physics. 17(38). 24917–24924. 44 indexed citations
7.
Toal, Siobhan, et al.. (2015). Randomizing the Unfolded State of Peptides (and Proteins) by Nearest Neighbor Interactions between Unlike Residues. Chemistry - A European Journal. 21(13). 5173–5192. 30 indexed citations
8.
Toal, Siobhan & Reinhard Schweitzer‐Stenner. (2014). Local Order in the Unfolded State: Conformational Biases and Nearest Neighbor Interactions. Biomolecules. 4(3). 725–773. 53 indexed citations
9.
Toal, Siobhan, et al.. (2014). The TrpA protein of Trichodesmium erythraeum IMS101 is a non-fibril-forming collagen and a component of the outer sheath. Microbiology. 160(10). 2148–2156. 3 indexed citations
10.
Schweitzer‐Stenner, Reinhard & Siobhan Toal. (2014). Entropy reduction in unfolded peptides (and proteins) due to conformational preferences of amino acid residues. Physical Chemistry Chemical Physics. 16(41). 22527–22536. 13 indexed citations
11.
Toal, Siobhan, Daniel Verbaro, & Reinhard Schweitzer‐Stenner. (2014). 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(5). 1309–1318. 45 indexed citations
12.
Toal, Siobhan, et al.. (2013). How do Nearest-Neighbor Interactions Effect the Conformational Distributions in Peptides?. Biophysical Journal. 104(2). 55a–55a.
13.
14.
Schweitzer‐Stenner, Reinhard, Andrew Hagarman, Siobhan Toal, Daniel Mathieu, & Harald Schwalbe. (2013). 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 Structure Function and Bioinformatics. 81(6). 955–967. 39 indexed citations
15.
Toal, Siobhan, et al.. (2013). 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(14). 3689–3706. 64 indexed citations
16.
Schweitzer‐Stenner, Reinhard, et al.. (2012). Structural Analysis of Unfolded Peptides by Raman Spectroscopy. Methods in molecular biology. 895. 315–346. 8 indexed citations
17.
Verbaro, Daniel, Daniel Mathieu, Siobhan Toal, Harald Schwalbe, & Reinhard Schweitzer‐Stenner. (2012). 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(28). 8084–8094. 15 indexed citations
18.
Toal, Siobhan, et al.. (2012). Triaspartate: A Model System for Conformationally Flexible DDD Motifs in Proteins. The Journal of Physical Chemistry B. 116(17). 5160–5171. 19 indexed citations
19.
Hagarman, Andrew, Daniel Mathieu, Siobhan Toal, et al.. (2011). Amino Acids with Hydrogen‐Bonding Side Chains have an Intrinsic Tendency to Sample Various Turn Conformations in Aqueous Solution. Chemistry - A European Journal. 17(24). 6789–6797. 51 indexed citations
20.
Toal, Siobhan, et al.. (2011). 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(32). 12728–12739. 29 indexed citations

Rankless uses publication and citation data sourced from OpenAlex, an open and comprehensive bibliographic database. While OpenAlex provides broad and valuable coverage of the global research landscape, it—like all bibliographic datasets—has inherent limitations. These include incomplete records, variations in author disambiguation, differences in journal indexing, and delays in data updates. As a result, some metrics and network relationships displayed in Rankless may not fully capture the entirety of a scholar's output or impact.

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