Amide proton hydrogen exchange rates for sperm whale myoglobin obtained from 15N-1H NMR spectra.

The hydrogen exchange behavior of exchangeable protons in proteins can provide important information for understanding the principles of protein structure and function. The positions and exchange rates of the slowly-exchanging amide protons in sperm whale myoglobin have been mapped using 15N-1H NMR...

Full description

Bibliographic Details
Main Authors: Cavagnero, S., Thériault, Y., Narula, S. S., Dyson, H. J., Wright, P. E.
Format: Text
Language:English
Published: Cold Spring Harbor Laboratory Press 2000
Subjects:
Research Article
Sperm whale
Online Access:http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2144433
http://www.ncbi.nlm.nih.gov/pubmed/10739261
Description
Summary:The hydrogen exchange behavior of exchangeable protons in proteins can provide important information for understanding the principles of protein structure and function. The positions and exchange rates of the slowly-exchanging amide protons in sperm whale myoglobin have been mapped using 15N-1H NMR spectroscopy. The slowest-exchanging amide protons are those that are hydrogen bonded in the longest helices, including members of the B, E, and H helices. Significant protection factors were observed also in the A, C, and G helices, and for a few residues in the D and F helices. Knowledge of the identity of slowly-exchanging amide protons forms the basis for the extensive quench-flow kinetic folding experiments that have been performed for myoglobin, and gives insights into the tertiary interactions and dynamics in the protein.

Similar Items