Temperature dependent structure of spider silk by X-ray diffraction
Source abstract
Abstract
We have investigated the structure of spider dragline silk by X-ray diffraction over a broad temperature range from room temperature up to thermal denaturation conditions. The dominating signal from the β-sheet crystallites is analyzed. Pronounced changes of scattering intensity starting at temperatures around 150 °C are observed. These changes are discussed in view of the respective lattice constants, crystal size, size distribution, crystallite number density and amino acid composition.
Source: openaire · Quality: candidate unverified · Source record ↗
Research context
OpenAlex topics: Silk-based biomaterials and applications · Biochemical and Structural Characterization · Phytochemical compounds biological activities
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References (23)
Show source-provided references
1. S.A. Fossey, D.L. Kaplan, Polymer Data Handbook, Chapt. “Silk Protein”, (Oxford University Press, 1999)
2. D.T. Grubb, L.W. Jelinski, Macromolecules 30, 2860 (1997)10.1021/ma961293c ↗
3. Z. Yang, D.T. Grubb, L.W. Jelinski, Macromolecules 30, 8254 (1997)10.1021/ma970548z ↗
4. B.L. Thiel, K.B. Guess, C. Viney, Biopolymers 41, 703 (1997)10.1002/(SICI)1097-0282(199706)41:7<703::AID-BIP1>3.0.CO;2-T ↗
5. J.M. Gosline, P.A. Guerette, C.S. Ortlepp, K.N. Savage, J. Exp. Biol. 202, 3295 (1999)10.1242/jeb.202.23.3295 ↗
6. C. Riekel, F. Vollrath, Int. J. Biol. Macromol. 29, 203 (2001)10.1016/S0141-8130(01)00166-0 ↗
7. J.D. van Beek, S. Hess, F. Vollrath, B.H. Meier, Proceedings of the National Academy of Sciences of the United States of America (PNAS) 99, 10266 (2002)10.1073/pnas.152162299 ↗
8. D. Huemmerich, U. Slotta, T. Scheibel, Appl. Phys. A 82, 219 (2006)10.1007/s00339-005-3428-5 ↗
9. C. Wong Po Foo, E. Bini, J. Huang, S.Y. Lee, D.L. Kaplan, Appl. Phys. A 82, 219 (2006)10.1007/s00339-005-3428-5 ↗
10. S. Rammensee, D. Huemmerich, K.D. Hermanson, T. Scheibel, A.R. Bausch, Appl. Phys. A 82, 219 (2006)10.1007/s00339-005-3431-x ↗
11. F. Vollrath, D. Porter, Appl. Phys. A 82, 219 (2006)10.1007/s00339-005-3437-4 ↗
12. J.P. Zbilut, T. Scheibel, D. Huemmerich, C.L. Webber, M. Colafranceschi, A. Guiliani, Appl. Phys. A 82, 219 (2006)10.1007/s00339-005-3429-4 ↗
13. P.M. Cunniff, S.A. Fossey, M.A. Auerbach, Polym. Advan. Technol. 5, 401 (1994)10.1002/pat.1994.220050801 ↗
14. K.B. Guess, C. Viney, Thermochim. Acta 315, 61 (1998)10.1016/S0040-6031(98)00277-9 ↗
15. J.O. Warwicker, J. Mol. Biol. 2, 350 (1960)10.1016/S0022-2836(60)80046-0 ↗
16. A. Glišović, T. Vehoff, R.J. Davies, T. Salditt, Strain Dependent Structure of Spider Dragline Silk by Single Fiber X-Ray Diffraction, to be published
17. R.W. Work, P.D. Emerson, J. Arachnology 10, 1 (1982)10.1016/0305-750X(82)90056-0 ↗
18. Y. Baskin, L. Meyer, Phys. Rev. 100, 2 (1955)10.1103/PhysRev.100.544 ↗
19. B.D. Cullity, Elements of X-Ray Diffraction, 2nd edn., (Addison-Wesley Publishing Company, London, 1978)
20. R.E. Marsh, R.B. Corey, L. Pauling, Biochim. Biophys. Acta 16 (1955)10.1016/0006-3002(55)90178-5 ↗
21. M. Xu, R.V. Lewis, Biochemistry 87, 7120 (1990)
22. M.B. Hinman, R.V. Lewis, J. Biol. Chem. 267, 19320 (1992)10.1016/S0021-9258(18)41777-2 ↗
23. H.S. Sheu, Int. J. Biol. Macromol. 34, 325 (2004)