High activity of Mj HSP16.5 under acidic condition

来源 :中国科学：化学英文版 | 被引量 : 0次 | 上传用户：tonnyliu2042

【摘要】

：

Small heat shock proteins (sHSPs) exist ubiquitously among all organisms, with a variety of functions. All small heat shock proteins assemble into a native larg

【作者】

：

Zheng Wang (1) AoNeng Cao (

【机构】

：

1.BeijingNationalLaboratoryforMolecularSciences,2.InstituteofNanochemistryandNanobiology

【出处】

：

中国科学：化学英文版

【发表日期】

：

2009年3期

【关键词】

：

small heat shock protein CHAPERONE MJ HSP16.5 DIMER ACIDIC FOLDING AGGREGATION s

【基金项目】

：

Supported by the National Natural Science Foundation of China (Grant Nos. 20203001, 20673003, and 30490245),Ministry of Science and Technology of China (Grant No. 2006AA02Z301)

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Small heat shock proteins (sHSPs) exist ubiquitously among all organisms, with a variety of functions. All small heat shock proteins assemble into a native large oligomeric state containing 9-40 monomers. The sHSPs show chaperone-like activity to prevent

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High activity of Mj HSP16.5 under acidic condition

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