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Structural dynamics of ligand diffusion in the protein matrix: A study on a new myoglobin mutant Y(B10) Q(E7) R(E10)Understanding a substrate's product regioselectivity in a family of enzymes: a case study of acetaminophen binding in cytochrome P450sThe effect of quaternary structure on the kinetics of conformational changes and nanosecond geminate rebinding of carbon monoxide to hemoglobin.Iron-carbonyl bond geometries of carboxymyoglobin and carboxyhemoglobin in solution determined by picosecond time-resolved infrared spectroscopy.Orientation of carbon monoxide and structure-function relationship in carbonmonoxymyoglobin.Relationships between structural dynamics and functional kinetics in oligomeric membrane receptorsBoth protein dynamics and ligand concentration can shift the binding mechanism between conformational selection and induced fitOxygen and CO binding to triply NO and asymmetric NO/CO hemoglobin hybrids.Experimental basis for a new allosteric model for multisubunit proteins.The effect of water on the rate of conformational change in protein allostery.Experiments on Hemoglobin in Single Crystals and Silica Gels Distinguish among Allosteric Models.Theory for rates, equilibrium constants, and Brønsted slopes in F1-ATPase single molecule imaging experiments.Steric control of CO binding in a totally synthetic heme protein modelSimulation of the kinetics of ligand binding to a protein by molecular dynamics: geminate rebinding of nitric oxide to myoglobin.Theory of single-molecule controlled rotation experiments, predictions, tests, and comparison with stalling experiments in F1-ATPaseApplication of linear free energy relations to protein conformational changes: the quaternary structural change of hemoglobin.Nanosecond absorption spectroscopy of hemoglobin: elementary processes in kinetic cooperativity.Mechanisms of cooperativity and allosteric regulation in proteins.Universality of supersaturation in protein-fiber formation.The role of hydration on the mechanism of allosteric regulation: in situ measurements of the oxygen-linked kinetics of water binding to hemoglobin.Temperature-dependent studies of NO recombination to heme and heme proteins.Kinetic and spectroscopic properties of the cyanide complexes of ferrous haemoglobins I and IV from trout blood.Measurements of heme relaxation and ligand recombination in strong magnetic fields.Photoactivation of the BLUF Protein PixD Probed by the Site-Specific Incorporation of Fluorotyrosine Residues.Site-directed mutagenesis in hemoglobinTheory of the diffusion-influenced substrate binding rate to a buried and gated active site
P2860
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P2860
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on May 1978
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Kinetics of hemoglobin and transition state theory.
@en
Kinetics of hemoglobin and transition state theory.
@nl
type
label
Kinetics of hemoglobin and transition state theory.
@en
Kinetics of hemoglobin and transition state theory.
@nl
prefLabel
Kinetics of hemoglobin and transition state theory.
@en
Kinetics of hemoglobin and transition state theory.
@nl
P2860
P356
P1476
Kinetics of hemoglobin and transition state theory.
@en
P2093
P2860
P304
P356
10.1073/PNAS.75.5.2108
P407
P577
1978-05-01T00:00:00Z