ROLE OF TRYPTOPHANYL RESIDUES IN DRIVING MYOGLOBIN FOLDING
https://doi.org/10.4081/jbr.2001.12504
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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). […]
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