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.
A soft and transparent handleable protein model
1. J. M. Berg, J. L. Tymoczko, and L. Stryer, Biochemistry, 5th ed. (Freeman, New York, 2002).
2. A. M. Wu and P. D. Senter, “Arming antibodies: prospects and challenges for immunoconjugates,” Nat. Biotechnol. 23, 1137 (2005).
3. G. Del Re, “Models and analogies in science,” HYLE: Int. J. Philos. Chem. 6, 5 (2000).
4. J. D. Watson and F. H. Crick, “Molecular structure of nucleic acids; a structure for deoxyribose nucleic acid,” Nature (London) 171, 737 (1953).
5. L. Pauling, The Nature of the Chemical Bond and the Structure of Molecules and Crystals (Cornell University Press, New York, 1960).
7. Editorial, “String and sealing wax,” Nat. Struct. Biol. 4, 961 (1997).
10. T. Herman, J. Morris, S. Colton, A. Batiza, M. Patrick, M. Franzen, and D. S. Goodsell, “Tactile teaching: Exploring protein structure/function using physical models,” Biochem. Mol. Biol. Educ. 34, 247 (2006).
11. G. A. Bain, J. Yi, M. Beikmohamadi, T. M. Herman, and M. A. Patrick, “Using physical models of biomolecular structures to teach concepts of biochemical structure and structure depiction in the introductory chemistry laboratory,” J. Chem. Educ. 83, 1322 (2006).
12. Housholder R. , “Molding process,” U.S. patent 4247508 (Jan 27, 1981).
13. R. Sayle and A. Bissell, in Proceedings of the 10th Eurographics UK ‘92 Conference (University of Edinburgh, Scotland, 1992).
15. E. F. Pettersen, T. D. Goddard, C. C. Huang, G. S. Couch, D. M. Greenblatt, E. C. Meng, and T. E. Ferrin, “UCSF Chimera–a visualization system for exploratory research and analysis,” J. Comput. Chem. 25, 1605 (2004).
18. T. J. Richmond, “Solvent accessible surface area and excluded volume in proteins: Analytical equations for overlapping spheres and implications for the hydrophobic effect,” J. Mol. Biol. 178, 63 (1984).
20. J. C. Kendrew, G. Bodo, H. M. Dintzis, R. G. Parrish, H. Wyckoff, and D. C. Phillips, “A three-dimensional model of the myoglobin molecule obtained by x-ray analysis,” Nature (London) 181, 662 (1958).
22. M. F. Perutz and J. Greer, “Stereochemical effects of amino acid substitution in abnormal human haemoglobin,” Biochem. J. 119, 31P (1970).
23. G. Fermi and M. F. Perutz, in Atlas on Molecular Structures in Biology, edited by D. C. Philips and F. M. Richards (Clarendon, Oxford, 1981), Vol. 2, 22–24.
26. S. Cooper, F. Khatib, A. Treuille, J. Barbero, J. Lee, M. Beenen, A. Leaver-Fay, D. Baker, Z. Popovic, and F. Players, “Predicting protein structures with a multiplayer online game,” Nature (London) 466, 756 (2010).
27. F. Khatib, F. DiMaio, S. Cooper, M. Kazmierczyk, M. Gilski, S. Krzywda, H. Zabranska, I. Pichova, J. Thompson, Z. Popovic, M. Jaskolski, and D. Baker, “Crystal structure of a monomeric retroviral protease solved by protein folding game players,” Nat. Struct. Mol. Biol. 18, 1175 (2011).
Article metrics loading...
The field of structural biology currently relies on computer-generated graphical representations of three-dimensional (3D) structures to conceptualize biomolecules. As the size and complexity of the molecular structure increases, model generation and peer discussions become more difficult. It is even more problematic when discussing protein–proteininteractions wherein large surface area contact is considered. This report demonstrates the viability of a new handleable protein molecular model with a soft and transparent silicone body similar to the molecule's surface. A full-color printed main chain structure embedded in the silicone body enables users to simultaneously feel the molecular surface, view through the main chain structure, and manually simulate molecular docking. The interactive, hands-on experience deepens the user's intuitive understanding of the complicated 3D proteinstructure and elucidates ligand binding and protein–proteininteractions. This model would be an effective discussion tool for the classroom or laboratory that stimulates inspired learning in this study field.
Full text loading...
Most read this month