Abstract:
:The structure of a new crystal form of leucine-enkephalin has been determined by X-ray diffraction. There are two independent molecules in the asymmetric unit and both have extended peptide backbone conformations with side-chains arranged alternately above and below the backbone planes. The two pentapeptides are hydrogen-bonded to each other and to other molecules forming an extended antiparallel beta-pleated sheet. The structure differs from that in similar crystals of methionine enkephalin primarily in side-chain orientations and inter-sheet interactions.
journal_name
Life Scijournal_title
Life sciencesauthors
Mastropaolo D,Camerman A,Ma LY,Camerman Ndoi
10.1016/0024-3205(87)90289-xsubject
Has Abstractpub_date
1987-05-18 00:00:00pages
1995-9issue
20eissn
0024-3205issn
1879-0631pii
0024-3205(87)90289-Xjournal_volume
40pub_type
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