Premium
Amide proton hydrogen exchange rates for sperm whale myoglobin obtained from 15 N‐ 1 H NMR spectra
Author(s) -
Cavagnero Silvia,
Thériault Yves,
Narula Surinder S.,
Dyson H. Jane,
Wright Peter E.
Publication year - 2000
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1110/ps.9.1.186
Subject(s) - myoglobin , sperm whale , amide , chemistry , folding (dsp implementation) , crystallography , proton , protein folding , proton nmr , protein structure , hydrogen bond , nuclear magnetic resonance spectroscopy , stereochemistry , molecule , biochemistry , organic chemistry , physics , quantum mechanics , electrical engineering , engineering
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 15 N‐ 1 H 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.