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Unraveling double stranded α‐helical coiled coils: An x‐ray diffraction study on hard α‐keratin fibers

Unraveling double stranded α‐helical coiled coils: An x‐ray diffraction study on hard α‐keratin fibers Transformations of proteins secondary and tertiary structures are generally studied in globular proteins in solution. In fibrous proteins, such as hard α‐keratin, that contain long and well‐defined double stranded α‐helical coiled coil domains, such study can be directly done on the native fibrous tissue. In order to assess the structural behavior of the coiled coil domains under an axial mechanical stress, wide angle x‐ray scattering and small angle x‐ray scattering experiments have been carried out on stretched horse hair fibers at relative humidity around 30%. Our observations of the three major axial spacings as a function of the applied macroscopic strain have shown two rates. Up to 4% macroscopic strain the coiled coils were slightly distorted but retained their overall conformation. Above 4% the proportion of coiled coil domains progressively decreased. The main and new result of our study is the observation of the transition from α‐helical coiled coils to disordered chains instead of the α‐helical coiled coil to β‐sheet transition that occurs in wet fibers. © 2001 John Wiley & Sons, Inc. Biopolymers 58: 526–533, 2001 http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Biopolymers Wiley

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