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Cover Picture: Crystal Structure of the DFNKF Segment of Human Calcitonin Unveils Aromatic Interactions between Phenylalanines (Chem. Eur. J. 9/2017)
Author(s) -
Bertolani Arianna,
Pizzi Andrea,
Pirrie Lisa,
Gazzera Lara,
Morra Giulia,
Meli Massimiliano,
Colombo Giorgio,
Gei Alessandro,
Cavallo Gabriella,
Terraneo Giancarlo,
Metrangolo Pierangelo
Publication year - 2017
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.201605297
Subject(s) - zipper , steric effects , chemistry , side chain , aromaticity , crystallization , crystallography , peptide , crystal structure , amyloid (mycology) , stereochemistry , molecule , biochemistry , organic chemistry , computer science , inorganic chemistry , algorithm , polymer
The amyloidogenic peptide, DFNKF , forms a steric zipper. Iodination of this widely studied sequence facilitated crystallization and allowed its high‐resolution single crystal structure determination for the first time. The structure unveils the importance of aromatic–aromatic interactions in stabilizing the amyloid self‐assembly. The amino acid side‐chains of facing β‐strands (shown in red and green, respectively) interdigitate like the teeth of a zipper, similar to that of blue jeans. More information can be found in the Full Paper by P. Metrangolo et al. on page 2051 ff.