Abstract
Structure-based protein models build a minimally frustrated energy landscape to focus on the influence of geometrical factors on their dynamics, and they have demonstrated that the native structure is often sufficient to determine the folding mechanism. We customize structure-based models with a flexible interaction potential to investigate this geometrical control of the folding pathway. In the case of SH3 a polarized transition state results from the delayed formation of the N-terminal beta sheet. We isolate the contributions of the native contact map, of chain connectivity and of excluded volume interactions to identify their roles in the creation of this specific mechanism. While the native contacts are a direct expression of the native structure we find that the unspecific repulsion is essential to understand how geometrical frustration guides the folding process.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
