The Influence of Two‐Dimensional Organization on Peptide Conformation |
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| Authors: | Dr Simon J White Dr Steven D Johnson Mark A Sellick Dr Agnieszka Bronowska Prof Peter G Stockley Prof Christoph Wälti |
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| Institution: | 1. Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds LS2 9JT (UK);2. Department of Electronics, University of York, York, Y010 5DD (UK);3. School of Electronic and Electrical Engineering, University of Leeds, Leeds LS2 9JT (UK);4. Heidelberg Institute for Theoretical Studies gGmbH, 69118 Heidelberg (Germany) |
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| Abstract: | Molecular crowding plays a significant role in regulating molecular conformation in cellular environments. It is also likely to be important wherever high molecular densities are required, for example in surface‐phase studies, in which molecular densities generally far exceed those observed in solution. Using on‐surface circular dichroism (CD) spectroscopy, we have investigated the structure of a synthetic peptide assembled into a highly packed monolayer. The immobilized peptide undergoes a structural transition between α‐helical and random coil conformation upon changes in pH and ionic concentration, but critically the threshold for conformational change is altered dramatically by molecular crowding within the peptide monolayer. This study highlights the often overlooked role molecular crowding plays in regulating molecular structure and function in surface‐phase studies of biological molecules. |
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| Keywords: | coiled coil molecular crowding circular dichroism peptide conformation surface analysis |
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