IB-CAS  > 中科院光生物学重点实验室
Probing the Lysine Proximal Microenvironments within Membrane Protein Complexes by Active Dimethyl Labeling and Mass Spectrometry
Zhou, Ye3; Wu, Yue5; Yao, Mingdong1; Liu, Zheyi3; Chen, Jin3; Chen, Jun1; Tian, Lirong3; Han, Guangye; Shen, Jian-Ren; Wang, Fangjun
2016
发表期刊ANALYTICAL CHEMISTRY
ISSN0003-2700
卷号88期号:24页码:12060-12065
摘要Positively charged lysines are crucial to maintaining the native structures of proteins and protein complexes by forming hydrogen bonds and electrostatic interactions with their proximal amino acid residues. However, it is still a challenge to develop an efficient method for probing the active proximal microenvironments of lysines without changing their biochemical/physical properties. Herein, we developed an active covalent labeling strategy combined with mass spectrometry to systematically probe the lysine proximal microenvironments within membrane protein complexes (similar to 700 kDa) with high throughput. Our labeling strategy has the advantages of high labeling efficiency and stability, preservation of the active charge states, as well as biological activity of the labeled proteins. In total, 121 lysines with different labeling levels were obtained for the photosystem II complexes from cyanobacteria, red algae, and spinach and provided important insights for understanding the conserved and nonconserved local structures of PSII complexes among evolutionarily divergent species that perform photosynthesis.
学科领域Chemistry, Analytical
DOI10.1021/acs.analchem.6b02502
收录类别SCI
语种英语
WOS关键词EVOLVING PHOTOSYSTEM-II ; CROSS-LINKED PEPTIDES ; STRUCTURAL-CHARACTERIZATION ; ELECTROSTATIC INTERACTION ; REDUCTIVE METHYLATION ; 33-KDA PROTEIN ; IDENTIFICATION ; CRYSTALLIZATION ; RESIDUES ; DYNAMICS
WOS研究方向Science Citation Index Expanded (SCI-EXPANDED)
WOS记录号WOS:000390621000015
出版者AMER CHEMICAL SOC
文献子类Article
出版地WASHINGTON
EISSN1520-6882
资助机构China State Key Basic Research Program Grant [2013CB911203] ; China State Key Research Grant [2016YFA0501402] ; National Natural Science Foundation of ChinaNational Natural Science Foundation of China (NSFC) [21675152, 21305139, 21573223] ; Youth Innovation Promotion Association of CAS [2014164] ; Strategic Priority Research Program of CAS [XDB17030100]
作者邮箱wangfj@dicp.ac.cn
引用统计
被引频次:26[WOS]   [WOS记录]     [WOS相关记录]
文献类型期刊论文
条目标识符http://ir.ibcas.ac.cn/handle/2S10CLM1/25291
专题中科院光生物学重点实验室
作者单位1.Chinese Acad Sci, Dalian Inst Chem Phys, Natl Chromatog R&A Ctr, Key Lab Separat Sci Analyt Chem, Dalian 116023, Peoples R China
2.Chinese Acad Sci, Energy Dalian Inst Chem Phys, Dalian Natl Lab Clean Energy, State Key Lab Catalysis, Dalian 116023, Peoples R China
3.Chinese Acad Sci, Inst Bot, Key Lab Photobiol, Beijing 100093, Peoples R China
4.Univ Chinese Acad Sci, Beijing 100049, Peoples R China
5.Okayama Univ, Grad Sch Nat Sci & Technol, Photosynth Res Ctr, 1-1,Naka 3 Chome, Okayama 7008530, Japan
6.Georgia Inst Technol, Sch Chem & Biochem, Atlanta, GA 30332 USA
推荐引用方式
GB/T 7714
Zhou, Ye,Wu, Yue,Yao, Mingdong,et al. Probing the Lysine Proximal Microenvironments within Membrane Protein Complexes by Active Dimethyl Labeling and Mass Spectrometry[J]. ANALYTICAL CHEMISTRY,2016,88(24):12060-12065.
APA Zhou, Ye.,Wu, Yue.,Yao, Mingdong.,Liu, Zheyi.,Chen, Jin.,...&Wang, Fangjun.(2016).Probing the Lysine Proximal Microenvironments within Membrane Protein Complexes by Active Dimethyl Labeling and Mass Spectrometry.ANALYTICAL CHEMISTRY,88(24),12060-12065.
MLA Zhou, Ye,et al."Probing the Lysine Proximal Microenvironments within Membrane Protein Complexes by Active Dimethyl Labeling and Mass Spectrometry".ANALYTICAL CHEMISTRY 88.24(2016):12060-12065.
条目包含的文件
文件名称/大小 文献类型 版本类型 开放类型 使用许可
acs.analchem.6b02502(3723KB)期刊论文出版稿开放获取CC BY-NC-SA浏览 请求全文
个性服务
推荐该条目
保存到收藏夹
查看访问统计
导出为Endnote文件
谷歌学术
谷歌学术中相似的文章
[Zhou, Ye]的文章
[Wu, Yue]的文章
[Yao, Mingdong]的文章
百度学术
百度学术中相似的文章
[Zhou, Ye]的文章
[Wu, Yue]的文章
[Yao, Mingdong]的文章
必应学术
必应学术中相似的文章
[Zhou, Ye]的文章
[Wu, Yue]的文章
[Yao, Mingdong]的文章
相关权益政策
暂无数据
收藏/分享
文件名: acs.analchem.6b02502.pdf
格式: Adobe PDF
此文件暂不支持浏览
所有评论 (0)
暂无评论
 

除非特别说明,本系统中所有内容都受版权保护,并保留所有权利。