Molekulare Struktur und Dynamik von Modellpeptiden und Protein G auf selbstorganisierten Monolagen
Final Report Abstract
The analysis of surface proteins remains a challenging task. This project has led to a new route towards solving protein structures on surfaces using a set of complementary surface analytical tools. SFG is a very powerful tool to probe proteins on surfaces, but its full potential can only be unleashed if combined with additional techniques. Each of these methods has their strengths and weaknesses, determining protein structure on surfaces requires piecing together bits of information from a range of different approaches. Using SFG, NEXAFS, ToF-SIMS, XPS and ssNMR conjointly we were able to determine the secondary structure, orientation and side chain structure of an lysine-leucine model peptide on a range of model surface. The developed methods were also used to study the orientation and structure of protein G and statherin on surfaces. The combination of surface analysis, ssNMR and specifically designed computer models guided and constrained by the experimental data provides a viable path towards protein structure determination on surfaces.
Publications
- A Solid-State Deuterium NMR and SFG Study of the Side Chain Dynamics of Peptides Adsorbed onto Surfaces. Journal of the American Chemical Society 131, 14148 (2009)
N. F. Breen, T. Weidner, K. Li, D. G. Castner, G. P. Drobny
- Assembly and Structure of α-Helical Peptide Films on Hydrophobic Fluorocarbon Surfaces. Biointerphases 5, 9 (2010)
T. Weidner, N. T. Samuel, K. McCrea, L. J. Gamble, R. S. Ward, D. G. Castner
- Probing Orientation and Conformation of α-Helix and β-Strand Model Peptides on Self-Assembled Monolayers Using Sum Frequency Generation and NEXAFS Spectroscopies. Langmuir 26, 3433 (2010)
T. Weidner, J. S. Apte, L. J. Gamble, D. G. Castner
- Sum Frequency Generation and Solid-State Nuclear Magnetic Resonance Study of the Structure, Orientation and Dynamics of Peptides Adsorbed onto Polystyrene Surfaces. Proceedings of the National Academy of Sciences of the USA, 107, 13288 (2010)
T. Weidner, N. F. Breen, K. Li, G. P. Drobny, D. G. Castner