Aromatic cross-strand ladders control the structure and stability of beta-rich peptide self-assembly mimics.

ABSTRACT: Though beta-rich self-assemblies comprise a major structural class of polypeptides, a detailed understanding of the determinants of their structure and stability is lacking. In particular, the roles of repetitive stretches of side chains running the long axis of these beta-sheets, termed "cross-strand ladders," remain poorly characterized due to the inherently insoluble and heterogeneous nature of self-assemblies. To overcome these experimental challenges, we have established a complementary experimental system termed "peptide self-assembly mimics" (PSAMs). The PSAMs capture a defined number of self-assembly-like peptide repeats within a soluble beta-rich protein, making structural and energetic studies possible. In this work, we investigated the role of cross-strand ladders containing aro

SUBMITTER: Biancalana M 

PROVIDER: S-EPMC2582519 | biostudies-literature | 2008 Oct

REPOSITORIES: biostudies-literature