Porphyrins are variously substituted tetrapyrrolic macrocycles, with wide-ranging biological
and chemical applications derived from metal chelation in the core and the 18π aromatic …

Heme-copper oxidases (HCOs) are terminal enzymes on the mitochondrial or bacterial
respiratory electron transport chain, which utilize a unique heterobinuclear active site to …

Conspectus Mononuclear nonheme iron–oxygen species, such as iron–superoxo,−
peroxo,− hydroperoxo, and− oxo, are key intermediates involved in dioxygen activation and …

An analytical formula has been derived for the calculation of the solvent accessible surface
area of a protein molecule or equivalently the surface area exterior to an arbitrary number of …

To determine how different amino acid sequences form similar protein structures, and how
proteins adapt to mutations that change the volume of residues buried in their close-packed …

The structural changes that occur on ligand binding to haemoglobin have been studied by
comparison of the atomic co-ordinates of human deoxy, horse met and human …

Presenting a wide-ranging view of current developments in protein research, the papers in
this collection, each written by highly regarded experts in the field, examine various aspects …

The structure of human oxyhaemoglobin was determined by single crystal X-ray analysis at
2· 1resolution. Data were collected on an Arndt-Wonacott camera at− 2° C. The structure …

DYNAMICS OF PROTEINS: ELEMENTS AND FUNCTION Page 1 Ann. Rev. Biochem. 1983.
53:263-30 Copyright © 1983 by Annual Reviews Inc. All rights reserved DYNAMICS OF …

The structure of oxymyoglobin has been refined at 1· 6 Å resolution, using diffractometer
data collected at− 12° C. The crystallographic R factor is 0· 159, and the atomic positions are …