Nature versus design: the conformational propensities of D-amino acids and the importance of side chain chirality.

ABSTRACT: D-amino acids are useful building blocks for de novo peptide design and they play a role in aging-related diseases associated with gradual protein racemization. For amino acids with achiral side chains, one should be able to presume that the conformational propensities of L- and D-amino acids are a reflection of one another due to the straightforward geometric inversion at the Cα atom. However, this presumption does not account for the directionality of the backbone dipole and the inverted propensities have never been definitively confirmed in this context. Furthermore, there is little known of how alternative side chain chirality affects the backbone conformations of isoleucine and threonine. Using a GGXGG host-guest pentapeptide system, we have completed exhaustive sampling of the confor

SUBMITTER: Towse CL 

PROVIDER: S-EPMC4204638 | biostudies-literature | 2014 Nov

REPOSITORIES: biostudies-literature