Optimization of a β-sheet-cap for long loop closure.

ABSTRACT: Protein loops make up a large portion of the secondary structure in nature. But very little is known concerning loop closure dynamics and the effects of loop composition on fold stability. We have designed a small system with stable β-sheet structures, including features that allow us to probe these questions. Using paired Trp residues that form aromatic clusters on folding, we are able to stabilize two β-strands connected by varying loop lengths and composition (an example sequence: RWITVTI - loop - KKIRVWE). Using NMR and CD, both fold stability and folding dynamics can be investigated for these systems. With the 16 residue loop peptide (sequence: RWITVTI-(GGGGKK)₂ GGGG-KKIRVWE) remaining folded (ΔG_U  = 1.6 kJ/mol at 295K). To increase stability and extend the serie

SUBMITTER: Anderson JM 

PROVIDER: S-EPMC7444092 | biostudies-literature | 2017 Mar

REPOSITORIES: biostudies-literature