This chapter reviews how allosteric (heterotrophic) effectors and natural mutations impact
hemoglobin (Hb) primary physiological function of oxygen binding and transport. First, an …

Haemoglobin (Hb) is widely known as the iron-containing protein in blood that is essential
for O 2 transport in mammals. Less widely recognised is that erythrocyte Hb belongs to a …

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 …

Forty years ago, a simple model of allosteric mechanisms (indirect interactions between
distinct sites), used initially to explain feedback-inhibited enzymes, was presented by …

Allostery is a biological phenomenon of fundamental importance in regulation and signaling,
and efforts to understand this process have led to the development of numerous models. In …

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 …

Hemoglobin (Hb) is a truly remarkable molecule. Human adult hemoglobin (Hb A) has a
tetrameric structure consisting of two α-chains with 141 amino acids each and two β-chains …

Allostery is the most direct and efficient way for regulation of biological macromolecule
function, ranging from the control of metabolic mechanisms to signal transduction pathways …

Hemoglobin (Hb) plays its vital role through structural and functional properties
evolutionarily optimized to work within red blood cells, ie, the tetrameric assembly, well …

Michaelis and Menten introduced to biochemistry the idea of time‐scale separation, in which
part of a system is assumed to be operating sufficiently fast compared to the rest so that it …