ROLE OF TRYPTOPHANYL RESIDUES IN DRIVING MYOGLOBIN FOLDING

Abstract

The detailed mechanism by which the primary sequence of a protein encodes its tertiary structure, and by which a protein spontaneously acquires its native fold, is still unclear. Myoglobin provides a good versatile system to investigate the factors that govern the rate and mechanism of protein folding. At neutral pH, myoglobin has a well-defined globular structure, comprising eight helical segments (A-H) packed to form a compact hydrophobic core where the heme group is bound (1,2). […]