title: Amide proton hydrogen exchange rates for sperm whale myoglobin obtained from 15N-1H NMR spectra.
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.
authors.affiliation: Department of Molecular Biology and Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, California 92037, USA.
authors.forename: S
authors.initials: S
authors.lastname: Cavagnero
authors.forename: Y
authors.initials: Y
authors.lastname: Thériault
authors.forename: S S
authors.initials: SS
authors.lastname: Narula
authors.forename: H J
authors.initials: HJ
authors.lastname: Dyson
authors.forename: P E
authors.initials: PE
authors.lastname: Wright
mesh_terms: D000577:Amides; D000818:Animals; D002021:Buffers; D003903:Deuterium; D009682:Magnetic Resonance Spectroscopy; D008297:Male; D008958:Models, Molecular; D009211:Myoglobin / Q000737:chemistry*; D009587:Nitrogen Isotopes; D011522:Protons; D013094:Spermatozoa / Q000737:chemistry*; D014907:Whales
chemical_list: D000577:Amides; D002021:Buffers; D009211:Myoglobin; D009587:Nitrogen Isotopes; D011522:Protons; D003903:Deuterium