Antiparallel β‐sheets in the crystal structure of the heptapeptide Met‐Glu‐His‐Phe‐Arg‐Trp‐Gly (ACTH 4–10)
- 1 February 1984
- journal article
- research article
- Published by Wiley in International Journal of Peptide and Protein Research
- Vol. 23 (2) , 151-157
- https://doi.org/10.1111/j.1399-3011.1984.tb02705.x
Abstract
The conformation of the molecules in ACTH 4-10 was determined as part of a study of the conformations of the biologically active N-terminal fragments of ACTH. ACTH 4-10 crystallizes in 2 different superstructures. The substructure considered in the present work is monoclinic, space group C2, a = 25.75 (1) .ANG., b = 27.78 (1) .ANG., c = 20.35 (1) .ANG., .beta. = 114.0 (1).degree., Z = 8 molecules ACTH 4-10 plus 22 weight percent solvent. The crystals contain antiparallel .beta.-sheets, the orientations of the side groups are not found, because of disorder. The present crystal structure and those of other linear oligopeptides emphasize that antiparallel .beta.-sheets are energetically favorable. It is very unlikely, however, that the ACTH 4-10 crystals contain the molecules in their biologically active form.Keywords
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