https://doi.org/10.4081/jbr.2001.12504
ROLE OF TRYPTOPHANYL RESIDUES IN DRIVING MYOGLOBIN FOLDING
Published: May 31, 2024
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All claims expressed in this article are solely those of the authors and do not necessarily represent those of their affiliated organizations, or those of the publisher, the editors and the reviewers. Any product that may be evaluated in this article or claim that may be made by its manufacturer is not guaranteed or endorsed by the publisher.
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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). […]
How to Cite
Sirangelo, I., Casillo, M., Malmo, C., & Irace, G. (2024). ROLE OF TRYPTOPHANYL RESIDUES IN DRIVING MYOGLOBIN FOLDING. Journal of Biological Research - Bollettino Della Società Italiana Di Biologia Sperimentale, 77(1-3). https://doi.org/10.4081/jbr.2001.12504
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