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

Published online by Cambridge University Press:  01 January 2000

SILVIA CAVAGNERO ,
YVES THÉRIAULT ,
SURINDER S. NARULA ,
H. JANE DYSON  and
PETER E. WRIGHT
SILVIA CAVAGNERO
Affiliation:
Department of Molecular Biology and Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, California 92037
YVES THÉRIAULT
Affiliation:
Department of Molecular Biology and Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, California 92037
SURINDER S. NARULA
Affiliation:
Department of Molecular Biology and Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, California 92037
H. JANE DYSON
Affiliation:
Department of Molecular Biology and Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, California 92037
PETER E. WRIGHT
Affiliation:
Department of Molecular Biology and Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, California 92037
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Abstract

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.

Keywords

hydrogen exchange rateproton-deuterium exchangereference data
Type
FOR THE RECORD
Information
Protein Science , Volume 9 , Issue 1 , January 2000 , pp. 186 - 193
Copyright
© 2000 The Protein Society

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