http://chineseinput.net/에서 pinyin(병음)방식으로 중국어를 변환할 수 있습니다.
변환된 중국어를 복사하여 사용하시면 됩니다.
On the mechanism of chaperone activity of the small heat-shock protein of Methanococcus jannaschii
Kim, Rosalind,Luhua Lai,Lee, Hi-Hong,Cheong, Gang-Won,Kim, Kyeong-Kyu,Zheng Wu,Hisao Yokota,Susan Marqusee,Kim, Sung-Hou Plant molecular biology and biotechnology research 2003 Plant molecular biology and biotechnology research Vol.2003 No.-
The small heat-shock protein (sHSP) from Methanococcus jannaschii (Mj HSP16.5) forms a homomeric complex of 24 subunits and has an overall structure of a multiwindowed hollow sphere with an external diameter of ≈120 Å and an internal diameter of ≈65 Å with six square "windows" of ≈17 Å across and eight triangular windows of ≈30 Å across. This sHSP has been known to protect other proteins from thermal denaturation. Using purified single-chain monellin as a substrate and a series of methods such as protease digestion, antibody binding, and electron microscopy, we show that the substrates bind to Mj HSP16.5 at a high temperature (80℃) on the outside surface of the sphere and are prevented from forming insoluble substrate aggregates in vitro. Circular dichroism studies suggest that a very small, if any, conformational change occurs in sHSP even at 80℃, but substantial conformational changes of the substrate are required for complex formation at 80℃. Furthermore, deletion mutation studies of Mj HSP16.5 suggest that the N-terminal region of the protein has no structural role but may play an important kinetic role in the assembly of the sphere by "preassembly condensation" of multiple monomers before final assembly of the sphere.