Two-dimensional NMR approaches to the study of protein structure and function.
Two-dimensional Fourier transform methods for homonuclear proton NMR spectroscopy have been introduced by Wüthrich and Ernst as a means of extending assignments in spectra of proteins. Multinuclear two-dimensional approaches also appear promising. We are applying current one- and two-dimensional NMR methods to protein family members that differ from one another by one or more amino acid substitutions. The overall goal is to elucidate relationships among the sequences, structures, and functions of these proteins: for example, to delineate primary structural requirements for changes in observable properties such as conformation, amino acid side chain dynamics, hydrogen exchange dynamics, pK'a values, and oxidation-reduction potentials. The ovomucoids from a variety of species of birds, which include a single set of 12 pairs of third-domain proteins (Mr = 6062 for turkey third domain, similar for others) that differ by single amino acid substitutions, provide a favorable system for the study of the structural and dynamic effects of single amino acid replacements. X-ray crystallographic structures of two ovomucoid third domains are available. Other series of proteins being studied by these methods include the photosynthetic electron transport proteins ferredoxin and plastocyanin.
D000595:Amino Acid Sequence; D000818:Animals; D008239:Lysine; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008958:Models, Molecular; D010059:Ovomucin; D011487:Protein Conformation; D011506:Proteins / Q000378:metabolism*; D014422:Turkeys
D011506:Proteins; D010059:Ovomucin; D008239:Lysine