W
Wim F. Vranken
Researcher at Vrije Universiteit Brussel
Publications - 128
Citations - 10430
Wim F. Vranken is an academic researcher from Vrije Universiteit Brussel. The author has contributed to research in topics: Protein structure & Structure validation. The author has an hindex of 37, co-authored 116 publications receiving 8560 citations. Previous affiliations of Wim F. Vranken include Université libre de Bruxelles & Ghent University.
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Journal ArticleDOI
The CCPN data model for NMR spectroscopy: Development of a software pipeline
Wim F. Vranken,Wayne Boucher,Tim J. Stevens,Rasmus H. Fogh,Anne Pajon,Miguel Llinás,Eldon L. Ulrich,John L. Markley,John Ionides,Ernest D. Laue +9 more
TL;DR: The development of a set of software applications that use the Data Model and its associated libraries, thus validating the approach and providing a pipeline for high‐throughput analysis of NMR data.
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ACPYPE - AnteChamber PYthon Parser interfacE
TL;DR: ACPYPE is a tool that simplifies the automatic generation of topology and parameters in different formats for different molecular mechanics programmes, including calculation of partial charges, while being object oriented for integration with other applications.
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Determination of secondary structure populations in disordered states of proteins using nuclear magnetic resonance chemical shifts.
TL;DR: It is shown that it is possible to obtain highly quantitative information about particularly important types of probability distributions, the populations of secondary structure elements (α-helix, β-strand, random coil, and polyproline II), by using the information provided by backbone chemical shifts.
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RECOORD: A recalculated coordinate database of 500+ proteins from the PDB using restraints from the BioMagResBank
Aart J. Nederveen,Jurgen F. Doreleijers,Wim F. Vranken,Zachary D. Miller,Chris A. E. M. Spronk,Sander B. Nabuurs,Peter Güntert,Miron Livny,John L. Markley,Michael Nilges,Eldon L. Ulrich,Robert Kaptein,Alexandre M. J. J. Bonvin +12 more
TL;DR: The set of recalculated coordinates constitutes a unified database of protein structures in which potential user‐ and software‐dependent biases have been kept as small as possible and can be used by the structural biology community for further development of calculation protocols, validation tools, structure‐based statistical approaches and modeling.
Journal ArticleDOI
PDBe: Protein Data Bank in Europe
Sameer Velankar,C. Best,B. Beuth,C. H. Boutselakis,N. D. Cobley,A. W. Sousa Da Silva,Dimitris Dimitropoulos,A. Golovin,Miriam Hirshberg,M. John,Eugene Krissinel,Richard H. Newman,Thomas J. Oldfield,Anne Pajon,Christopher J. Penkett,J. Pineda-Castillo,Gaurav Sahni,Sanchayita Sen,Robert A. Slowley,A. Suarez-Uruena,J. Swaminathan,G. van Ginkel,Wim F. Vranken,Kim Henrick,Gerard J. Kleywegt +24 more
TL;DR: The PDBe web pages that describe individual PDB entries have been enhanced through the introduction of plain-English summary pages and iconic representations of the contents of an entry (PDBprints); the entire web site has been redesigned to make it substantially easier to use for expert and novice users alike.