Demo Data from EDBT 2026 / reviewers in the wild / expert
D. P. Klose
dblp:35/8713
· DBLP profile ↗
1ranked-venue papers
1as first author
0since 2021 · last 2010
—ORCID · none
Domains — the database's venue-derived domains; a paper can count in several
Applied, interdisciplinary, general and emerging computing · 1 · 1 first-author
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
| Topic | Weight | Papers | Last | Evidence papers |
|---|---|---|---|---|
Bioinformatics and computational biology
protein structure analysis |
0.1 | 1 | 2010 | 2Struc: the secondary structure server · Bioinform. 2010 |
Bioinformatics and computational biology › protein structure analysis › protein secondary structure analysis
secondary structure assignment |
0.1 | 1 | 2010 | 2Struc: the secondary structure server · Bioinform. 2010 |
Bioinformatics and computational biology
structural bioinformatics |
0.1 | 1 | 2010 | 2Struc: the secondary structure server · Bioinform. 2010 |
Methods — techniques the papers use, named apart from their topics
crystal structures · 0.1NMR models · 0.1DSSP · 0.1
| Year | Publication | Venue | Position |
|---|---|---|---|
| 2010 | 2Struc: the secondary structure serverabstractSUMMARY: The defined secondary structure of proteins method is often considered the gold standard for assignment of secondary structure from three-dimensional coordinates. However, there are alternative methods. '2Struc: The Secondary Structure Server' has been created as a single point of access for eight different secondary structure assignment methods. It has been designed to enable comparisons between methods for analyzing the secondary structure content for a single protein. It also includes a second functionality, 'Compare-the-Protein' to enable comparisons of the secondary structure features from any one method to be made within a collection of nuclear magnetic resonance models, or between the crystal structures of two different proteins. AVAILABILITY: http://2struc.cryst.bbk.ac.uk CONTACT: [email protected] SUPPLEMENTARY INFORMATION: Supplementary data are available at Bioinformatics online. D. P. Klose, B. A. Wallace, Robert W. Janes |
Bioinform. | 1 |