Abstract
The tail sheath of T-even bacteriophages is one of the simplest contractile structures. It is shown, by circular dichroism, optical rotatory dispersion and infrared spectroscopy, that a contraction of the bacteriophage T4 sheath results in a change of the sheath protein subunit secondary structure. This change consists of a decrease in the α -helical content and an increase in the β -form content. Quantitative evaluations of the revealed change of the secondary structure are reported.
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