Abstract
The effects of the position of charged amino acid side chains on the stability of the alpha-helix are investigated. Calculations for the model polyAla 13 residue alpha-helix, with modifications based on experimental work, are performed at three levels of approximation. The observed stabilization of the alpha-helix could be explained by interactions between its macrodipole and charged amino acid side chains. Limitations of the model are discussed.
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.
