scispace - formally typeset
G

Geerten W. Vuister

Researcher at University of Leicester

Publications -  136
Citations -  21798

Geerten W. Vuister is an academic researcher from University of Leicester. The author has contributed to research in topics: Protein structure & Structure validation. The author has an hindex of 49, co-authored 133 publications receiving 20798 citations. Previous affiliations of Geerten W. Vuister include Radboud University Nijmegen Medical Centre & Radboud University Nijmegen.

Papers
More filters
Journal ArticleDOI

NMRPipe: a multidimensional spectral processing system based on UNIX pipes

TL;DR: The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks.
Journal ArticleDOI

Quantitative J correlation: a new approach for measuring homonuclear three-bond J(HNH.alpha.) coupling constants in 15N-enriched proteins

TL;DR: A new approach is described for the measurement of homonuclear H N -H α J couplings in 15 N-enriched proteins, which relies on measurement of the diagonal-peak to cross-peak intensity ratio in a 3D15 N-separated quantitative J-correlation spectrum.
Journal ArticleDOI

Resolution enhancement and spectral editing of uniformly 13C-enriched proteins by homonuclear broadband 13C decoupling

TL;DR: In this article, the authors demonstrate that high resolution in the 13C spectrum can be obtained in an efficient manner by using a "constant-time" 13C evolution period, where the effect of 13C15N J coupling can be removed in a straightforward manner by the use of broadband 15N decoupling.
Book ChapterDOI

Measurement of homo- and heteronuclear J couplings from quantitative J correlation

TL;DR: Quantitative J correlation is a useful and general approach for measuring a large variety of two- and three-bond homo- and heteronuclear J couplings, providing access to the study of a large number of dihedral angles in proteins.
Journal ArticleDOI

CcpNmr AnalysisAssign: a flexible platform for integrated NMR analysis

TL;DR: CcpNmr version-3, the latest software release from the Collaborative Computational Project for NMR, is presented, designed to be simple, functional and flexible, and aims to ensure that routine tasks can be performed in a straightforward manner.