Subunit architecture of silkworm small heat shock protein and its temperature- dependent change
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چکیده
Introduction Abrupt increase in environmental temperature induces the expression of a variety of small heat shock protein (sHSP) genes. sHSP is a family of proteins having an αcrystalline domain and suppressing the thermal aggregation of other proteins. sHSP19.9 and sHSP20.8 are two of six sHSPs from the silkworm, Bombyx mori. Each is composed of identical polypeptides, and each of polypeptides has a single cysteine residue: Cys-123 and Cys-43 in sHSP19.9 and sHSP20.8, respectively. In both sHSPs, some sulfhydryl groups remain free, others form inter-subunit disulfide bonds [1,2]. However, little is known about their assembly structures. This paper reports structural characteristics of sHSP19.9 and sHSP20.8 at 30C measured by small-angle x-ray scattering (SAXS).
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تاریخ انتشار 2008