Water molecules can control the side-chain rotamer distribution of an aryl peptide in a nonpolar environment.
With computer-controlled circular dichroism (CD) spectrophotometry it is possible to obtain difference CD spectra which result from small perturbations to the environment of a chiral molecule. In the experiments described here a dry iso-octane solution of cyclobis-N-methyl-L-phenylalanine (c-(NMe-L-Phe)2) has been perturbed by exposure to water vapor. The resulting difference spectrum shows that water coordination to c-(NMe-L-Phe)2 eliminates negative ellipticity in the 244 nm region, while it simultaneously creates positive CD intensity in the 212 nm region. These two features of the difference spectrum plus related features of other direct spectra imply that water coordinated with p-orbital unpaired electrons of the carbonyl interferes sterically with the chi = 180 degrees side-chain rotamer. It can be expected that in this way hydrogen bonding of any species to backbone carbonyls can control the rotamer distribution of aromatic side-chains, if one of the rotamers occludes unpaired electrons of the carbonyl. Such control may offer an on-off switch for electron transport through proteins.
Radding
W
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Department of Physiology & Biophysics, University of Alabama, Birmingham 35294.
D002942:Circular Dichroism; D003196:Computer Graphics; D008958:Models, Molecular; D010456:Peptides, Cyclic; D010649:Phenylalanine / Q000031:analogs & derivatives*; D011487:Protein Conformation; D014867:Water
D010456:Peptides, Cyclic; D014867:Water; D010649:Phenylalanine; C057221:cyclobis(N-methylphenylalanine)