Chinese Journal of Magnetic Resonance

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Solid-State NMR Studies on Amyloid Fibrils: Recent Progresses

ZHANG Zheng-feng1,2, YANG Jun1*   

  1. 1. State Key Laboratory of Magnetic Resonance and Atomic and Molecular Physics, Wuhan Center of Magnetic Resonance (Wuhan Institute of Physics and Mathematics, Chinese Academy of Sciences), Wuhan 430071, China;
    2. University of Chinese Academy of Sciences, Beijing 100049, China
  • Received:2012-05-24 Revised:2012-06-19 Online:2013-06-05 Published:2013-06-05
  • About author:张正逢(1985-),男,江西泰和人,博士研究生,主要从事蛋白质的固体核磁共振研究. *通讯联系人:杨俊,电话:027-87199723,E-mail:yangjun@wipm.ac.cn.
  • Supported by:

    国家自然科学基金资助项目(21075133).

Abstract:

Amyloid fibrils are fibriform aggregates of amyloid proteins, which are implicated in many protein deposition diseases. Knowing the structures of amyloid fibrils will shed light on the molecular mechanism of fibrillation, facilitating the prevention and therapy of related diseases. Solid-state NMR is the most prospective technique for elucidating the structures of amyloid fibrils, since they are insoluble and non-crystalline such that they are difficult to be studied by liquid-state NMR and X-ray diffraction approaches. In this paper, recent progresses on using solid-state NMR methods to elucidate structural information of proteins, especially amyloid fibrils, are reviewed.

Key words: solid-state NMR, amyloid fibril, three-dimensional structure, magic angle spinning, protein, secondary structure

CLC Number: