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RISS 인기검색어
- 검색키워드
- 저자 : Susan Marqusee (검색결과 2 건)
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Solution Structure of a Prion Protein: Implications for Infectivity
He Liu,Shauna Farr-Jones,Nikolai Ulyanov,Manuel Llinas,Susan Marqusee,Fred E. Cohen,Stanley B. Prusiner,Thomas L. James 한국자기공명학회 1998 Journal of the Korean Magnetic Resonance Society Vol.2 No.2
Prions cause neurodegenerative diseases in animals and humans. The scrapie prion protein (PrPSc) is the major – possibly only – component of the infectious prion and is generated from the cellular isoform (PrPC) by a conformational change. Limited proteolysis of PrPSc produces a polypeptide comprised primarily of residues 90 to 231, which retains infectivity. The three-dimensional structure of rPrP(90-231), a recombinant protein resembling PrPC with the Syrian hamster (SHa) sequence, was solved using multidimensional NMR. Low-resolution structures of rPrP(90-231), synthetic peptides up to 56 residues, a longer (29-231, full-length) protein with SHa sequence, and a shorter (121-231) protein with the mouse sequence have been previously reported. We report here further structure refinement of rPrP(90-231) and dynamic features of the protein. Consideration of these features in the context of published data suggests regions of conformational heterogeneity, structural elements involved in the PrPC PrPSc transformation, and possible structural features related to a species barrier to transmission of prion diseases 영어논문
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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.
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