title: Experimental evaluation of CH-π interactions in a protein core.
abstract: 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.
authors.affiliation: Department of Chemistry, Merkert Chemistry Center, Boston College, 2609 Beacon Street, Chestnut Hill, MA 02467, USA.
authors.forename: Christopher J
authors.initials: CJ
authors.lastname: Pace
authors.forename: Diane
authors.initials: D
authors.lastname: Kim
authors.forename: Jianmin
authors.initials: J
authors.lastname: Gao
mesh_terms: D008958:Models, Molecular; D010649:Phenylalanine / Q000031:analogs & derivatives* / Q000737:chemistry*; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*; D013816:Thermodynamics; D014867:Water
chemical_list: D011506:Proteins; D014867:Water; C028544:cyclohexylalanine; D010649:Phenylalanine