Journal ArticleDOI
Backbone dynamics of Escherichia coli ribonuclease HI: correlations with structure and function in an active enzyme.
TLDR
In this article, the intramolcular dynamical properties of E. coli coliribonuclease H, including spin-lattic relaxation rate, spin-spin relaxation rate constants, and steady state nuclear Overhauser effects for the 15N nuclear spins were measured by using proton-detected heteronuclear NMR spectroscopy.About:
This article is published in Journal of Molecular Biology.The article was published on 1995-02-10. It has received 972 citations till now. The article focuses on the topics: RNase H & Ribonuclease.read more
Citations
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Journal ArticleDOI
A hierarchy of timescales in protein dynamics is linked to enzyme catalysis.
Katherine A. Henzler-Wildman,Ming Lei,Vu Hong Thai,S. Jordan Kerns,Martin Karplus,Dorothee Kern +5 more
TL;DR: It is shown that pico- to nano-second timescale atomic fluctuations in hinge regions of adenylate kinase facilitate the large-scale, slower lid motions that produce a catalytically competent state.
Book ChapterDOI
Nuclear magnetic resonance methods for quantifying microsecond-to-millisecond motions in biological macromolecules.
Journal ArticleDOI
Structural disorder of monomeric α-synuclein persists in mammalian cells
Francois-Xavier Theillet,Francois-Xavier Theillet,Andres Binolfi,Andres Binolfi,Beata Bekei,Andrea Martorana,Honor May Rose,Marchel Stuiver,Silvia Verzini,Dorothea Lorenz,Marleen van Rossum,Daniella Goldfarb,Philipp Selenko +12 more
TL;DR: It is established that different types of crowded intracellular environments do not inherently promote α-synuclein oligomerization and, more generally, that intrinsic structural disorder is sustainable in mammalian cells.
Journal ArticleDOI
Two-state allosteric behavior in a single-domain signaling protein.
TL;DR: A strong correlation is found between phosphorylation-driven activation of the signaling protein NtrC and microsecond time-scale backbone dynamics and a dynamic population shift between two preexisting conformations as the underlying mechanism of activation.
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