Back to search

Application of linear free energy relations to protein conformational changes: the quaternary structural change of hemoglobin.

Data up to Jan 2025

Published1991
Citations75
References35

Total Citations Per Year

Abstract

References (35)

On the nature of allosteric transitions: A plausible model

1965 • 8,699 citations

Stereochemistry of Cooperative Effects in Haemoglobin: Haem–Haem Interaction and the Problem of Allostery

1970 • 2,874 citations

Kinetics and Mechanism

1961 • 2,376 citations

Chemical kinetics and dynamics

1989 • 1,432 citations

Structural invariants in protein folding

1975 • 865 citations

Haemoglobin: The structural changes related to ligand binding and its allosteric mechanism

1979 • 862 citations

Parameters for the Description of Transition States

1953 • 542 citations

Mechanisms of cooperativity and allosteric regulation in proteins

1990 • 514 citations

Hemoglobin: Structure, function, evolution, and pathology

1984 • 507 citations

Kinetics and mechanism

1985 • 504 citations

The photochemical formation of a quickly reacting form of haemoglobin

1959 • 269 citations

Quaternary conformational changes in human hemoglobin studied by laser photolysis of carboxyhemoglobin.

1976 • 262 citations

A mathematical model for structure-function relations in hemoglobin

1972 • 255 citations

Allosteric Effects in Haemoglobin

1982 • 246 citations

Allosteric interpretation of haemoglobin properties

1975 • 210 citations

Nanosecond absorption spectroscopy of hemoglobin: elementary processes in kinetic cooperativity.

1983 • 207 citations

Cooperative Interactions of Hemoglobin

1975 • 160 citations

PH dependence of the Adair constants of human hemoglobin. Nonuniform contribution of successive oxygen bindings to the alkaline Bohr effect.

1975 • 143 citations

Crystals of haemoglobin with the T quaternary structure bind oxygen noncooperatively with no Bohr effect

1991 • 114 citations

Kinetics of hemoglobin and transition state theory.

1978 • 106 citations

Nanosecond optical spectra of iron-cobalt hybrid hemoglobins: geminate recombination, conformational changes, and intersubunit communication

1985 • 96 citations

Energetics of subunit assembly and ligand binding in human hemoglobin

1980 • 73 citations

Analysis of proton release in oxygen binding by hemoglobin: implications for the cooperative mechanism

1988 • 63 citations

The effect of quaternary structure on the kinetics of conformational changes and nanosecond geminate rebinding of carbon monoxide to hemoglobin.

1988 • 61 citations

The balance sheet of a hemoglobin

1977 • 55 citations

Allosteric Effects in Hemoglobin

1967 • 53 citations

Quaternary conformational changes in human oxyhemoglobin studied by laser photolysis.

1977 • 52 citations

Optically Detected Conformational Changes in Haemoglobin Single Crystals

1974 • 45 citations

Reaction pathway for the quaternary structure change in hemoglobin

1985 • 41 citations

Thermodynamic analysis of carbon monoxide binding by hemoglobin trout I

1979 • 40 citations

Testing the two-state model: anomalous effector binding to human hemoglobin

1986 • 27 citations

Conformational kinetics of triligated hemoglobin

1985 • 23 citations

Spin equilibrium and quaternary structure change in hemoglobin A. Experiments on a quantitative probe of the stereochemical mechanism of hemoglobin cooperativity

1979 • 22 citations

Rate of allosteric change in hemoglobin measured by modulated excitation using fluorescence detection

1989 • 16 citations

Allosteric kinetics and equilibria differ for carbon monoxide and oxygen binding to hemoglobin

1990 • 10 citations

Cited By (0)

Loading...
Application of linear free energy relations to protein conformational changes: the… (1991) – Proceedings of the National Academy of Sciences | Metascience Observatory Explorer