scispace - formally typeset
R

Robert Kaptein

Researcher at Utrecht University

Publications -  437
Citations -  25223

Robert Kaptein is an academic researcher from Utrecht University. The author has contributed to research in topics: CIDNP & Nuclear magnetic resonance spectroscopy. The author has an hindex of 72, co-authored 436 publications receiving 24275 citations. Previous affiliations of Robert Kaptein include University of Groningen & University of Amsterdam.

Papers
More filters
Journal ArticleDOI

AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR

TL;DR: The AQUA and PROCHECK-NMR programs provide a means of validating the geometry and restraint violations of an ensemble of protein structures solved by solution NMR, and their outputs include a detailed breakdown of the restraint violations.
Journal ArticleDOI

Solution structure of the glucocorticoid receptor DNA-binding domain

TL;DR: A model of the dimeric complex between the DBD and the glucocorticoid response element is proposed, consistent with previous results indicating that specific amino acid residues of the D BD are involved in protein-DNA and protein-protein interactions.
Journal ArticleDOI

Structure and Flexibility Adaptation in Nonspecific and Specific Protein-DNA Complexes

TL;DR: The solution structure and dynamics of the complex of a dimeric lac repressor DNA binding domain with nonspecific DNA is reported, showing that the protein-DNA interface of the nonspecial complex is flexible on biologically relevant time scales that may assist in the rapid and efficient finding of the target site.
Journal ArticleDOI

The Nisin-Lipid II Complex Reveals a Pyrophosphate Cage that Provides a Blueprint for Novel Antibiotics

TL;DR: The structure shows a novel lipid II–binding motif in which the pyrophosphate moiety of lipid II is primarily coordinated by the N-terminal backbone amides of nisin via intermolecular hydrogen bonds, which provides a rationale for the conservation of the lanthionine rings among several lipid II-binding lantibiotics.
Journal ArticleDOI

A protein structure from nuclear magnetic resonance data. Lac Repressor headpiece

TL;DR: This procedure combines model building with a restrained molecular dynamics algorithm, in which distance information from nuclear Overhauser effects is incorporated in the form of pseudo potentials, to determine the three-dimensional structure of biomolecules from nuclear magnetic resonance data.