Structural and kinetic characterization of the simplified SH3 domain FP1

• DOI: 10.1110/ps.0238603
• Publication Date: 2003-03-20T20:05:09Z
• Authors: Qian Yi; Ponni Rajagopal; Rachel E. Klevit; David Baker
• Keywords: src Homology Domains; Kinetics; 0303 health sciences; 03 medical and health sciences; Magnetic Resonance Spectroscopy; Mutation

The simplified SH3 domain sequence, FP1, obtained in phage display selection experiments has an amino acid composition that is 95% Ile, Lys, Glu, Ala, Gly. Here we use NMR to investigate the tertiary structure of FP1. We find overall topology FP1 resembles src domain, hydrogen-deuterium exchange and chemical shift perturbation profiles are similar those naturally occurring domains, (15)N relaxation rates range small proteins. Guided by structure, further simplify sequence compare effects on folding kinetics point mutations wild-type domain. results suggest transition state but somewhat less polarized than