Skip to main content

News about Scitation

In December 2016 Scitation will launch with a new design, enhanced navigation and a much improved user experience.

To ensure a smooth transition, from today, we are temporarily stopping new account registration and single article purchases. If you already have an account you can continue to use the site as normal.

For help or more information please visit our FAQs.

banner image
No data available.
Please log in to see this content.
You have no subscription access to this content.
No metrics data to plot.
The attempt to load metrics for this article has failed.
The attempt to plot a graph for these metrics has failed.
The full text of this article is not currently available.
1. M. Cretich, F. Damina, G. Pirria, and M. Chiari, Biomol. Eng. 23, 77 (2006).
2. L. S. Wong, F. Khan, and J. Micklefield, Chem. Rev. 109, 4025 (2009).
3. N. Adam, The Physics and Chemistry of Surfaces (Oxford University Press, London, 1941).
4. M. T. Smith, J. C. Wu, C. T. Varner, and B. C. Bundy, Biotechnol. Prog. 29, 247 (2013).
5. S.-W. Hung, P.-Y. Hsiao, M.-C. Lu, and C.-C. Chieng, J. Phys. Chem. B 116, 12661 (2012).
6. R. B. Pandey, Z. Kuang, B. L. Farmer, S. S. Kim, and R. R. Naik, Soft Matter 8, 9101 (2012).
7. S. Wei and T. A. Knotts IV, J. Chem. Phys. 139, 095102 (2013).
8. S. Wei and T. A. Knotts IV, J. Chem. Phys. 133, 115102 (2010).
9. S. Wei and T. A. Knotts IV, J. Chem. Phys. 134, 185101 (2011).
10. T. A. Knotts IV, N. Rathore, and J. J. de Pablo, Proteins 61, 385 (2005).
11. M. Friedel, A. Baumketner, and J. Shea, Proc. Natl. Acad. Sci. U.S.A. 103, 8396 (2006).
12. Z. Zhuang, A. I. Jewett, P. Soto, and J.-E. Shea, Phys. Biol. 6, 015004 (2009).
13. H. M. Berman, J. Westbrook, Z. Feng, G. Gilliland, T. N. Bhat, H. Weissig, I. N. Shindyalov, and P. E. Bourne, Nucl. Acids Res. 28, 235 (2000).
14. A. L. Cuff, I. Sillitoe, T. Lewis, O. C. Redfern, R. Garratt, J. Thornton, and C. A. Orengo, Nucl. Acids Res. 37, D310 (2009).
15. C. Orengo, A. Michie, D. Jones, M. Swindells, and J. Thornton, Structure 5, 1093 (1997).
16. D. Frishman and P. Argos, Proteins 23, 566 (1995).
17. W. Humphrey, A. Dalke, and K. Schulten, J. Mol. Graph. 14, 33 (1996).
18. J. I. Lewis, D. J. Moss, and T. A. Knotts IV, J. Chem. Phys. 136, 245101 (2012).
19. J. C. Wu, C. H. Hutchings, M. J. Lindsay, C. J. Werner, and B. C. Bundy, “Enhanced enzyme stability through site-directed covalent immobilization,” J. Biotechnol. (unpublished).
20.See supplementary material at for simulation details. [Supplementary Material]
21. J. Karanicolas and C. L. Brooks III, J. Mol. Biol. 334, 309 (2003).
22. T. J. Schmitt, J. E. Clark, and T. A. Knotts IV, J. Chem. Phys. 131, 235101 (2009).

Data & Media loading...


Article metrics loading...



Protein surface interactions are important in many applications in biotechnology including protein arrays, but these technologies have not lived up to their transformative potential because it is difficult to attach proteins to surfaces in a manner that preserves function and theoretical understanding of the relevant phenomena remains limited. Here is reported the effect of using multiple tethers to attach a protein (lysozyme) to a surface and the effects on the structure and stability of the molecule. The simulations show how using two tethers can drastically change the folding mechanism such that a protein that is initially unstable and inactive when attached using a single tether can become more stable and functional when two tethers are used. The results offer hope that the rational design of protein arrays is possible.


Full text loading...


Access Key

  • FFree Content
  • OAOpen Access Content
  • SSubscribed Content
  • TFree Trial Content
752b84549af89a08dbdd7fdb8b9568b5 journal.articlezxybnytfddd