A proton nuclear magnetic resonance study of the antihypertensive and antiviral protein BDS-I from the sea anemone Anemonia sulcata: sequential and stereospecific resonance assignment and secondary structure.
The sequential resonance assignment of the 1H NMR spectrum of the antihypertensive and antiviral protein BDS-I from the sea anemone Anemonia sulcata is presented. This is carried out with two-dimensional NMR techniques to identify through-bond and through-space (less than 5 A) connectivities. Added spectral complexity arises from the fact that the sample is an approximately 1:1 mixture of two BDS-I isoproteins, (Leu-18)-BDS-I and (Phe-18)-BDS-I. Complete assignments, however, are obtained, largely due to the increased resolution and sensitivity afforded at 600 MHz. In addition, the stereospecific assignment of a large number of beta-methylene protons is achieved from an analysis of the pattern of 3J alpha beta coupling constants and the relative magnitudes of intraresidue NOEs involving the NH, C alpha H, and C beta H protons. Regular secondary structure elements are deduced from a qualitative interpretation of the nuclear Overhauser enhancement, 3JHN alpha coupling constant, and amide NH exchange data. A triple-stranded antiparallel beta-sheet is found to be related to that found in partially homologous sea anemone polypeptide toxins.
Driscoll
P C
PC
Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, Bethesda, Maryland 20892.
Clore
G M
GM
Beress
L
L
Gronenborn
A M
AM
D000595:Amino Acid Sequence; D000818:Animals; D000959:Antihypertensive Agents; D000998:Antiviral Agents; D003064:Cnidarian Venoms; D004735:Energy Transfer; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D011487:Protein Conformation; D012615:Sea Anemones
D000959:Antihypertensive Agents; D000998:Antiviral Agents; C059796:BDS-I antiviral protein, Anemonia sulcata; D003064:Cnidarian Venoms