Distal pocket residues affect picosecond ligand recombination in myoglobin. An experimental and molecular dynamics study of position 29 mutants.
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The role of cavities in protein dynamics: Crystal structure of a photolytic intermediate of a mutant myoglobinLigand migration in human myoglobin: steric effects of isoleucine 107(G8) on O(2) and CO binding.Influence of distal residue B10 on CO dynamics in myoglobin and neuroglobinImaging the migration pathways for O2, CO, NO, and Xe inside myoglobin.Competition with xenon elicits ligand migration and escape pathways in myoglobin.Myoglobin mutants giving the largest geminate yield in CO rebinding in the nanosecond time domainApplication of the primary hydration shell approach to locally enhanced sampling simulated annealing: computer simulation of thyrotropin-releasing hormone in waterHuman myoglobin recognition of oxygen: dynamics of the energy landscape.Ligand dissociation from estrogen receptor is mediated by receptor dimerization: evidence from molecular dynamics simulationsPi release from myosin: a simulation analysis of possible pathways.Molecular dynamics simulations reveal multiple pathways of ligand dissociation from thyroid hormone receptors.Extended subnanosecond structural dynamics of myoglobin revealed by Laue crystallography.Solvation and cavity occupation in biomolecules.Fluorescent protein barrel fluctuations and oxygen diffusion pathways in mCherry.O2 migration pathways are not conserved across proteins of a similar fold.Application of molecular dynamics and free energy perturbation methods to metalloporphyrin-ligand systems II: CO and dioxygen binding to myoglobinSimulation of the kinetics of ligand binding to a protein by molecular dynamics: geminate rebinding of nitric oxide to myoglobin.Exploring the diffusion of molecular oxygen in the red fluorescent protein mCherry using explicit oxygen molecular dynamics simulations.Time-resolved flow-flash FT-IR difference spectroscopy: the kinetics of CO photodissociation from myoglobin revisited.Ligand diffusion in globins: simulations versus experiment.The transition from inhomogeneous to homogeneous kinetics in CO binding to myoglobin.Rate of nitric oxide scavenging by hemoglobin bound to haptoglobin.Computer simulations of carbon monoxide photodissociation in myoglobin: structural interpretation of the B states.Disentangling ligand migration and heme pocket relaxation in cytochrome P450cam.Temperature-dependent studies of NO recombination to heme and heme proteins.Multiphoton absorption of myoglobin-nitric oxide complex: relaxation by D-NEMD of a stationary state.Cavities and packing defects in the structural dynamics of myoglobin.Kinetics of CO Recombination to the Heme in Geobacillus Stearothermophilus Nitric Oxide Synthase.Solvent Composition Drives the Rebinding Kinetics of Nitric Oxide to Microperoxidase.
P2860
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P2860
Distal pocket residues affect picosecond ligand recombination in myoglobin. An experimental and molecular dynamics study of position 29 mutants.
description
1992 nî lūn-bûn
@nan
1992 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
1992 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
1992年の論文
@ja
1992年論文
@yue
1992年論文
@zh-hant
1992年論文
@zh-hk
1992年論文
@zh-mo
1992年論文
@zh-tw
1992年论文
@wuu
name
Distal pocket residues affect ...... study of position 29 mutants.
@ast
Distal pocket residues affect ...... study of position 29 mutants.
@en
type
label
Distal pocket residues affect ...... study of position 29 mutants.
@ast
Distal pocket residues affect ...... study of position 29 mutants.
@en
prefLabel
Distal pocket residues affect ...... study of position 29 mutants.
@ast
Distal pocket residues affect ...... study of position 29 mutants.
@en
P2093
P1476
Distal pocket residues affect ...... study of position 29 mutants.
@en
P2093
P304
22022-22034
P407
P577
1992-11-01T00:00:00Z