The native state of apomyoglobin described by proton NMR spectroscopy: the A-B-G-H interface of wild-type sperm whale apomyoglobin.

doi:10.1002/(SICI)1097-0134(199607)25:3<267::AID-PROT1>3.0.CO;2-D

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Article

The native state of apomyoglobin described by proton NMR spectroscopy: the A-B-G-H interface of wild-type sperm whale apomyoglobin.

Proteins - 1 Jul 1996

Lecomte J T, Kao Y H, Cocco M J

Abstract excerpt

Proton nuclear magnetic resonance spectroscopy was applied to sperm whale apomyoglobin to describe the conformation adopted by the protein under native conditions. The study focused on the A-B-G-H interface, a region known to form a compact subdomain in the apoprotein (Hughson and Baldwin, Bioche...

Topics

Animals
Apoproteins
Magnetic Resonance Spectroscopy
Mutation
Myoglobin
Protein Conformation
Protons
Whales

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