Retention of Native Quaternary Structure in Racemic Melittin Crystals.

ABSTRACT: Racemic crystallography has been used to elucidate the secondary and tertiary structures of peptides and small proteins that are recalcitrant to conventional crystallization. It is unclear, however, whether racemic crystallography can capture native quaternary structure, which could be disrupted by heterochiral associations. We are exploring the use of racemic crystallography to characterize the self-assembly behavior of membrane-associated peptides, very few of which have been crystallized. We report a racemic crystal structure of the membrane-active peptide melittin; the new structure allows comparison with a previously reported crystal structure of L-melittin. The tetrameric assembly observed in crystalline L-melittin has been proposed to represent the tetrameric state detected in solut

SUBMITTER: Kurgan KW 

PROVIDER: S-EPMC6520119 | biostudies-literature | 2019 May

REPOSITORIES: biostudies-literature