Rotational dynamics and transition mechanisms of surface-adsorbed proteins

• DOI: 10.1073/pnas.2020242119
• Publication Date: 2022-04-13T09:53:06Z
• Authors: Shuai Zhang; Robbie Sadre; Benjamin A. Legg; Harley Pyles; Talita Perciano; E. Wes Bethel; David Baker; Oliver Rübel; James J. De Yoreo
• Keywords: Energy landscape; Maxima and minima; Biomolecule; Rotational energy; Kinetic Monte Carlo

Assembly of biomolecules at solid–water interfaces requires molecules to traverse complex orientation-dependent energy landscapes through processes that are poorly understood, largely due the dearth in situ single-molecule measurements and statistical analyses rotational dynamics define directional selection. Emerging capabilities high-speed atomic force microscopy machine learning have allowed us directly determine orientational landscape observe quantify for protein nanorods on surface muscovite mica under a variety conditions. Comparisons with kinetic Monte Carlo simulations show transition rates between adjacent orientation-specific energetic minima can be understood traditional models in-plane Brownian rotation across biased landscape, resulting exponential barriers states. However, transitions more distant angular states decoupled from barrier height, jump-size distributions showing power law decay is characteristic nonclassical Levy-flight random walk, indicating large jumps enabled by alternative modes motion via activated The findings provide insights into solid–liquid lead self-assembly, epitaxial matching, other orientationally anisotropic outcomes general procedure exploring such implications hybrid biomolecular–inorganic materials design.