Although phenomenlogical models that account for cooperativity in allosteric systems date
back to the early and mid‐60's (eg, the KNF and MWC models), there is resurgent interest in …

The molecular mechanism of O 2 binding to hemoglobin (Hb) has been critically reviewed
on the basis of the information built up in the last decades. It allows to describe in detail from …

Introduction to Proteins provides a comprehensive and state-of-the-art introduction to the
structure, function, and motion of proteins for students, faculty, and researchers at all levels …

The aim of the book is to introduce the reader to the kinetic analysis of a wide range of
biological processes at the molecular level. It is intended to show that the same approach …

Initiation of protein folding by light can dramatically improve the time resolution of kinetic
studies. Here we present an example of an optically triggered folding reaction by using …

Revised Manuscript Received January 13, 1994® abstract: Absorption spectroscopy with
nanosecond time resolution shows that myoglobin undergoes conformational relaxation on …

The two-state allosteric model of Monod, Wyman, and Changeux (MWC) provides an
excellent description of homotropic effects in a vast array of equilibrium and kinetic …

Fast-folding proteins have been a major focus of computational and experimental study
because they are accessible to both techniques: they are small and fast enough to be …

We compare various allosteric models that have been proposed to explain cooperative
oxygen binding to hemoglobin, including the two‐state allosteric model of Monod, Wyman …

Recent functional studies reported on human adult hemoglobin (HbA) show that heterotropic
effector-linked tertiary structural changes are primarily responsible for modulating the …