TY - JOUR
T1 - Sequential 1H‐NMR assignments and secondary structure of the sea anemone polypeptide anthopleurin‐A
AU - MABBUTT, Bridget C.
AU - NORTON, Raymond S.
PY - 1990
Y1 - 1990
N2 - The sequence‐specific assignment of resonances in the 500‐MHz 1H‐NMR spectrum of a cardioactive sea anemone polypeptide, anthopleurin‐A, is described. The assignment procedure involved analysis of two‐dimensional phase‐sensitive multiple‐quantum‐filtered, double‐quantum, homonuclear Hartmann‐Hahn and nuclear Overhauser effect spectra. Using sequential information, specific assignments have been made for resonances arising from all 49 amino acid residues. Resonances arising from a number of residues in a minor conformer present in solution are also assigned. These results greatly extend previous resonance assignments made from spectra acquired at 300 MHz [Gooley, P. R. and Norton, R. S. (1985) Eur. J. Biochem. 153, 529–539] and provide the basis for a more accurate definition of the conformation of anthopleurin‐A in aqueous solution. The secondary structure includes a four‐stranded antiparallel β‐sheet encompassing residues 2–4, 21–23, 34–36 and 45–49, and possibly a β‐bulge located at Ser‐19 and Gly‐20. A type II β‐turn is formed by residues 30–33. These structural elements also occur within other related sea anemone polypeptides, but the conformation of the small loop region containing Pro‐41 appears to be unique to anthopleurin‐A.
AB - The sequence‐specific assignment of resonances in the 500‐MHz 1H‐NMR spectrum of a cardioactive sea anemone polypeptide, anthopleurin‐A, is described. The assignment procedure involved analysis of two‐dimensional phase‐sensitive multiple‐quantum‐filtered, double‐quantum, homonuclear Hartmann‐Hahn and nuclear Overhauser effect spectra. Using sequential information, specific assignments have been made for resonances arising from all 49 amino acid residues. Resonances arising from a number of residues in a minor conformer present in solution are also assigned. These results greatly extend previous resonance assignments made from spectra acquired at 300 MHz [Gooley, P. R. and Norton, R. S. (1985) Eur. J. Biochem. 153, 529–539] and provide the basis for a more accurate definition of the conformation of anthopleurin‐A in aqueous solution. The secondary structure includes a four‐stranded antiparallel β‐sheet encompassing residues 2–4, 21–23, 34–36 and 45–49, and possibly a β‐bulge located at Ser‐19 and Gly‐20. A type II β‐turn is formed by residues 30–33. These structural elements also occur within other related sea anemone polypeptides, but the conformation of the small loop region containing Pro‐41 appears to be unique to anthopleurin‐A.
UR - http://www.scopus.com/inward/record.url?scp=0025193220&partnerID=8YFLogxK
U2 - 10.1111/j.1432-1033.1990.tb15337.x
DO - 10.1111/j.1432-1033.1990.tb15337.x
M3 - Article
C2 - 1968006
AN - SCOPUS:0025193220
SN - 0014-2956
VL - 187
SP - 555
EP - 563
JO - European Journal of Biochemistry
JF - European Journal of Biochemistry
IS - 3
ER -