Crystal structure of an extended-conformation leucine-enkephalin dimer monohydrate.

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 Sci

journal_title

Life sciences

authors

Mastropaolo D,Camerman A,Ma LY,Camerman N

doi

10.1016/0024-3205(87)90289-x

subject

Has Abstract

pub_date

1987-05-18 00:00:00

pages

1995-9

issue

20

eissn

0024-3205

issn

1879-0631

pii

0024-3205(87)90289-X

journal_volume

40

pub_type

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