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Distance dependency of exciton coupled circular dichroism using turn and helical peptide spacers
Author(s) -
Oancea Simona,
Formaggio Fernando,
Campestrini Sandro,
Broxterman Quirinus B.,
Kaptein Bernard,
Toniolo Claudio
Publication year - 2003
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.10315
Subject(s) - circular dichroism , chemistry , chromophore , porphyrin , turn (biochemistry) , crystallography , exciton , peptide , stereochemistry , photochemistry , biochemistry , physics , quantum mechanics
Porphyrins are promising chromophores for the investigation of the still unexplored area of 3‐dimensional structural studies of proteins by using the exciton coupled circular dichroism (CD) method. The synthesis, conformational characterization by FTIR absorption and 1 H‐NMR, and CD properties are described for a model bis ‐porphyrin system based on homooligo‐[ L ‐(αMe)Val] n peptides as rigid spacers. In particular, the coupled CD phenomenon is experimentally detected, the intensity of which is modulated by the interchromophoric distance. These results extend and integrate those already reported with steroid, dimeric steroid, and brevetoxin bridges. © 2003 Wiley Periodicals, Inc. Biopolymers (Biospectroscopy) 72: 105–115, 2003