about
Watching a signaling protein function in real time via 100-ps time-resolved Laue crystallographyTertiary and Quaternary Allostery in Tetrameric Hemoglobin from Scapharca inaequivalvisEstimating free-energy barrier heights for an ultrafast folding protein from calorimetric and kinetic data.Relaxation rate for an ultrafast folding protein is independent of chemical denaturant concentration.A statistical mechanical model for beta-hairpin kinetics.Measuring internal friction of an ultrafast-folding proteinChemical, physical, and theoretical kinetics of an ultrafast folding protein.The effect of quaternary structure on the kinetics of conformational changes and nanosecond geminate rebinding of carbon monoxide to hemoglobin.Is cooperative oxygen binding by hemoglobin really understood?Simulation of the kinetics of ligand binding to a protein by molecular dynamics: geminate rebinding of nitric oxide to myoglobin.Evolution of allosteric models for hemoglobin.Comparing a simple theoretical model for protein folding with all-atom molecular dynamics simulations.Can a two-state MWC allosteric model explain hemoglobin kinetics?Crystals of haemoglobin with the T quaternary structure bind oxygen noncooperatively with no Bohr effectNanosecond crystallographic snapshots of protein structural changesTheoretical Simulation of Red Cell Sickling Upon Deoxygenation Based on the Physical Chemistry of Sickle Hemoglobin Fiber FormationAllosteric control of hemoglobin S fiber formation by oxygen and its relation to the pathophysiology of sickle cell disease
P50
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P50
description
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Eric R Henry
@ast
Eric R Henry
@en
Eric R Henry
@es
Eric R Henry
@nl
Eric R Henry
@sl
type
label
Eric R Henry
@ast
Eric R Henry
@en
Eric R Henry
@es
Eric R Henry
@nl
Eric R Henry
@sl
prefLabel
Eric R Henry
@ast
Eric R Henry
@en
Eric R Henry
@es
Eric R Henry
@nl
Eric R Henry
@sl
P106
P1153
7102238438
P31
P496
0000-0002-5648-8696