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Impact of Strand Number on Parallel β‐Sheet Stability
Author(s) -
Kung Vanessa M.,
Cornilescu Gabriel,
Gellman Samuel H.
Publication year - 2015
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201506448
Subject(s) - cooperativity , beta sheet , circular dichroism , nuclear magnetic resonance spectroscopy , folding (dsp implementation) , stability (learning theory) , aqueous solution , chemistry , crystallography , spectroscopy , materials science , chemical physics , nuclear magnetic resonance , physics , stereochemistry , protein structure , computer science , engineering , structural engineering , quantum mechanics , machine learning , biochemistry
We have examined whether parallel β‐sheet secondary structure becomes more stable as the number of β‐strands increases, via comparisons among peptides designed to adopt two‐ or three‐stranded parallel β‐sheet conformations in aqueous solution. Our three‐strand design is the first experimental model of a triple‐stranded parallel β‐sheet. Analysis of the designed peptides by nuclear magnetic resonance (NMR) and circular dichroism (CD) spectroscopy supports the hypothesis that increasing the number of β‐strands, from two to three, increases the stability of the parallel β‐sheet. We present the first experimental evidence for cooperativity in the folding of a triple‐stranded parallel β‐sheet, and we show how minimal model systems may enable experimental documentation of characteristic properties, such as CD spectra, of parallel β‐sheets.