Regensburg 2016 – wissenschaftliches Programm
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BP: Fachverband Biologische Physik
BP 23: Posters - Protein Structure and Dynamics
BP 23.3: Poster
Montag, 7. März 2016, 17:30–19:30, Poster C
On the α-Helical Coiled Coil to β-Sheet Conversion in Regenerated Hornet Silk — •Andreas Schaper1, Taiyo Yoshioka2, Tsunenori Kameda2, Kohji Tashiro3, Takashi Nemoto4, and Tetsuya Ogawa4 — 1Philipps University, Marburg, Germany — 2National Institute of Agrobiological Sciences, Tsukuba, Japan — 3Toyota Technological Institute, Nagoya, Japan — 4Kyoto University, Uji, Japan
Alpha-helices, alpha-helical coiled coils and β-sheets are fundamental principles of chain folding in fiber-forming proteins. Evolution has been creating numbers of different structures by varying the intrinsic properties of the amino acid sequences as well as the pathway the fibrillar structures are produced. Studies of protein denaturation as it is initiated by solvents, inappropriate pH level, elevated temperature or other forms of stress, including mechanical deformation and distortion, are key for solving fundamental questions regarding the stability of native α-helix structures and their tendency to undergo amyloid or amyloid-like structure formations under non-physiological conditions.
Resuming our recent studies of the structural details of native silk from the hornet Vespa mandarinia [1], here we report X-ray and electron diffraction observations of regenerated silk under different drawing regimes. We succeeded in evaluating the transformation from a dominant four-strand alpha-helical coiled coil [1,2] to an advanced twisted cross-beta state.
[1] T. Kameda et al., J. Struct. Biol. 185, 303 (2014); [2] R.D.B. Fraser and D.A.D. Parry, J. Struct. Biol. 192, 528 (2015)