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Thomas Gurry

dblp:184/4837 · DBLP profile ↗
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1ranked-venue papers
0as first author
0since 2021 · last 2016
—ORCID · unresolved

Domains — the database's venue-derived domains; a paper can count in several

Applied, interdisciplinary, general and emerging computing · 1

Expertise — from the expertise taxonomy: the topics of the expert's papers under the CCF categories. A weight counts papers with recency: 1 for a paper about the topic, 0.3 when the topic is its context, halved every five years.

Interdisciplinary, comprehensive, and emerging computing
1 paper
Bioinformatics and computational biology · 100%

Topics — the 3 heaviest of 3, each with the papers that count most for it

TopicWeightPapersLastEvidence papers
Bioinformatics and computational biology › computational structural biology
conformational ensemble generation
0.212016
Mollack: a web server for the automated creation of conformational ensembles for intrinsically disordered proteins · Bioinform. 2016
Bioinformatics and computational biology › protein structure analysis
intrinsically disordered protein
0.212016
Mollack: a web server for the automated creation of conformational ensembles for intrinsically disordered proteins · Bioinform. 2016
Bioinformatics and computational biology › structural bioinformatics
protein structure
0.212016
Mollack: a web server for the automated creation of conformational ensembles for intrinsically disordered proteins · Bioinform. 2016

Methods — techniques the papers use, named apart from their topics

molecular simulation · 0.2
YearPublicationVenuePosition
2016 Mollack: a web server for the automated creation of conformational ensembles for intrinsically disordered proteins
abstract
UNLABELLED: Intrinsically disordered proteins (IDPs) play central roles in many biological processes. Consequently, an accurate description of the disordered state is an important step towards a comprehensive understanding of a number of important biological functions. In this work we describe a new web server, Mollack, for the automated construction of unfolded ensembles that uses both experimental and molecular simulation data to construct models for the unfolded state. An important aspect of the method is that it calculates a quantitative estimate of the uncertainty in the constructed ensemble, thereby providing an objective measure of the quality of the final model. Overall, Mollack facilitates structure-function studies of disordered proteins. AVAILABILITY AND IMPLEMENTATION: http://cmstultz-mollack.mit.edu CONTACT: [email protected] SUPPLEMENTARY INFORMATION: Supplementary data are available at Bioinformatics online.
Zachary Ziegler, Molly Schmidt, Thomas Gurry, Virginia Burger, Collin M. Stultz
Bioinform.3