Abstract

Attenuated total reflection Fourier transform infrared (ATR/FT-IR) spectra of wet horse hair α-keratin indicate that the conformation of extended α-keratin is affected by the water temperature. Extension of the wet horse hair in 21 °C water gives rise to parallel β-sheet structures, thus suggesting that the original α-helical structure is also parallel. In contrast, extension of the wet horse hair α-keratin in 95 °C water gives rise to anti-parallel β-sheet structures (consistent with reported literature where X-ray diffraction was used), suggesting that disulfide interchange and/or increased chain mobility at elevated temperatures plays a role in altering the secondary structure.

PDF Article

Cited By

You do not have subscription access to this journal. Cited by links are available to subscribers only. You may subscribe either as an OSA member, or as an authorized user of your institution.

Contact your librarian or system administrator
or
Login to access OSA Member Subscription