Hydrophobic interactions are a major driving force in the folding of globular proteins and aggregation of non-globular proteins. The villin headpiece-36 (HP36) is an ideal model to study these hydrophobic residue interactions and dynamics due to its small size and cooperative folding. Three phenylalanine residues, F47, F51, and F58, form the base of the hydrophobic core of HP36. Here, we report a study of the sidechain rotation of F58 under different hydration (144%, 40%, 10%) levels in the solid powder state. The potential mean forces for the dihedral are computed through umbrella sampling. These results were compared to experimental solid-state NMR results which provided activation energy barriers for ring-flipping motion under around 5% and 40% hydrated powder states. The study offers insights into hydrophobic core dynamics and structural stability of HP36 and other protein.

Computational study on the effect of hydration on the dynamics of the villin headpiece subdomain HP36

Macromolecular Chemistry: The Second Century

[Author Benefits](https://scimeetings.acs.org/?utm_source=pubs_content_marketing&utm_medium=website&utm_campaign=0320_MCF_NPI_Launch_Spring_Homepage&ref=pubs_content_marketing)

[How to use SciMeetings](https://storage.googleapis.com/dl.morressier.com/acs/SciMeetings-ACSSpring2020-HowToGuide_M3020-Final.pdf)

[Frequently Asked Questions](https://storage.googleapis.com/dl.morressier.com/acs/SciMtng_ACSNMSp2020_FAQ_M3120_Final.pdf)

ACS Spring 2020 National Meeting & Expo

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.