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Experimental Evaluation of CH–π Interactions in a Protein Core
Author(s) -
Pace Christopher J.,
Kim Diane,
Gao Jianmin
Publication year - 2012
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.201200334
Subject(s) - stacking , limit (mathematics) , core (optical fiber) , stability (learning theory) , content (measure theory) , computer science , chemistry , crystallography , combinatorics , information retrieval , physics , mathematics , telecommunications , organic chemistry , mathematical analysis , machine learning
CH–π stacks up! Using the protein α 2 D as a model system, we estimate that a CH–π contact between cyclohexylalanine (Cha) and phenylalanine (F) contributes approximately −0.7 kcal mol −1 to the protein stability. The stacking F–Cha pairs are sequestered in the core of the protein, where water interference does not exist (see figure). Therefore, the observed energetic gain should represent the inherent magnitude and upper limit of the CH–π interactions.