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András Perczel

dblp:55/1640 · DBLP profile ↗
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2ranked-venue papers
0as first author
0since 2021 · last 2008
0000-0003-1252-6416ORCID · corroborated

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

Applied, interdisciplinary, general and emerging computing · 2

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
2 papers
Bioinformatics and computational biology · 100%

Topics — the 4 heaviest of 4, each with the papers that count most for it

TopicWeightPapersLastEvidence papers
Bioinformatics and computational biology › structural bioinformatics
protein structure determination
0.112008
Fast protein fold estimation from NMR-derived distance restraints · Bioinform. 2008
Bioinformatics and computational biology › protein analysis › protein bioinformatics
protein family
0.012004
A simple fold with variations: the pacifastin inhibitor family · Bioinform. 2004
Bioinformatics and computational biology › structural bioinformatics
protein structure
0.012004
A simple fold with variations: the pacifastin inhibitor family · Bioinform. 2004
Bioinformatics and computational biology › structural biology › protein structure and function
protein stability
0.012004
A simple fold with variations: the pacifastin inhibitor family · Bioinform. 2004

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

NMR distance restraints · 0.1structural analysis · 0.0
YearPublicationVenuePosition
2008 Fast protein fold estimation from NMR-derived distance restraints
abstract
Abstract Summary: PRIDE-NMR is a fast novel method to relate known protein folds to NMR distance restraints. It can be used to obtain a first guess about a structure being determined, as well as to estimate the completeness or verify the correctness of NOE data. Availability: The PRIDE-NMR server is available at http://www.icgeb.org/pride Contact: [email protected] Supplementary information: Description of the server and details of the tests presented can be found at http://www.icgeb.org/pride
Annamária F. Ángyán, András Perczel, Sándor Pongor, Zoltán Gáspári
Bioinform.2
2004 A simple fold with variations: the pacifastin inhibitor family
abstract
Members of the pacifastin family are small, approximately 35-residue serine protease inhibitors isolated from arthropod species. Several locust inhibitors exhibit intriguing taxon specificity while others do not. The structural basis of this phenomenon may lie in the different dynamical properties of the proteins originating from different stabilizing interactions. In this study, we identify new members of the family to confirm the universal role of these interactions in the family. Structural investigations show that both the disulfide pattern and the stabilizing interactions are unique among small all-beta proteins.
Zoltán Gáspári, Csaba P. Ortutay, András Perczel
Bioinform.3