Multiple isomers and protonation sites of the phenylalanine/serine dimer.
Our investigation of the phenylalanine/serine (Phe/Ser) protonated dimer suggests that the intermolecular interaction between the two amino acids is more complex than could have been anticipated from previous studies of similar systems. Isomer-specific infrared (IR) spectra, recorded at an internal temperature of ~10 K, demonstrate the presence of at least five isomers with nonzwitterionic structures. Moreover, isotopic substitution experiments provide evidence for different protonation sites among these isomers.
Laboratoire de Chimie Physique Moléculaire, École Polytechnique Fédérale de Lausanne, CH-1015 Lausanne, Switzerland.
Ulrich J
UJ
Lorenz
Thomas R
TR
Rizzo
D019281:Dimerization; D007536:Isomerism; D010649:Phenylalanine / Q000737:chemistry*; D011522:Protons; D012694:Serine / Q000737:chemistry*; D013055:Spectrophotometry, Infrared
D011522:Protons; D012694:Serine; D010649:Phenylalanine