Amide proton hydrogen exchange rates for sperm whale myoglobin obtained from 15N-1H NMR spectra |
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Authors: | Cavagnero S Thériault Y Narula S S Dyson H J Wright P E |
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Affiliation: | Department of Molecular Biology and Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, California 92037, USA. |
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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. |
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Keywords: | hydrogen exchange rate proton-deuterium exchange reference data |
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