about
Insights into domain-domain motions in proteins and RNA from solution NMRCapturing a Dynamic Chaperone-Substrate Interaction Using NMR-Informed Molecular ModelingToward a unified representation of protein structural dynamics in solution.Inter-helical conformational preferences of HIV-1 TAR-RNA from maximum occurrence analysis of NMR data and molecular dynamics simulations.Measuring similarity between dynamic ensembles of biomoleculesDefining conformational ensembles of intrinsically disordered and partially folded proteins directly from chemical shifts.Efficient in silico exploration of RNA interhelical conformations using Euler angles and WExploreIntrinsic disorder in measles virus nucleocapsids.Engineering a therapeutic lectin by uncoupling mitogenicity from antiviral activityModulating RNA Alignment Using Directional Dynamic Kinks: Application in Determining an Atomic-Resolution Ensemble for a Hairpin using NMR Residual Dipolar Couplings.Advances in the determination of nucleic acid conformational ensemblesA general method for constructing atomic-resolution RNA ensembles using NMR residual dipolar couplings: the basis for interhelical motions revealed.Visualizing chaperone-assisted protein folding.Nuclear magnetic resonance provides a quantitative description of protein conformational flexibility on physiologically important time scales.Characterizing weak protein-protein complexes by NMR residual dipolar couplings.Towards a robust description of intrinsic protein disorder using nuclear magnetic resonance spectroscopy.Investigating protein conformational energy landscapes and atomic resolution dynamics from NMR dipolar couplings: a review.Quantitative description of backbone conformational sampling of unfolded proteins at amino acid resolution from NMR residual dipolar couplings.Activity of Tumor Necrosis Factor α Is Modulated by Dynamic Conformational Rearrangements.The Mechanism of HdeA Unfolding and Chaperone Activation.Flexible-meccano: a tool for the generation of explicit ensemble descriptions of intrinsically disordered proteins and their associated experimental observables.Protein conformational flexibility from structure-free analysis of NMR dipolar couplings: quantitative and absolute determination of backbone motion in ubiquitin.Dynamic Descriptions of Highly Flexible Molecules from NMR Dipolar Couplings: Physical Basis and Limitations.NMR characterization of long-range order in intrinsically disordered proteins.HdeB functions as an acid-protective chaperone in bacteria.Structure, Dynamics, and Kinetics of Weak Protein-Protein Complexes from NMR Spin Relaxation Measurements of Titrated SolutionsMapping the population of protein conformational energy sub-states from NMR dipolar couplings
P50
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P50
description
researcher, ORCID id # 0000-0002-0249-6279
@en
wetenschapper
@nl
name
Loic Salmon
@ast
Loic Salmon
@en
Loic Salmon
@es
Loic Salmon
@nl
type
label
Loic Salmon
@ast
Loic Salmon
@en
Loic Salmon
@es
Loic Salmon
@nl
prefLabel
Loic Salmon
@ast
Loic Salmon
@en
Loic Salmon
@es
Loic Salmon
@nl
P106
P31
P496
0000-0002-0249-6279