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| Probing the Proteomics Dark Regions by VAILase Cleavage at Aliphatic Amino Acids | |
| Sun, Binwen1; Liu, Zheyi; Fang, Zheng1; Dong, Wei2; Yu, Yang3,4; Ye, Mingliang; Liu, Lin2; Wang, Hongda3,4; Wang, Fangjun1 | |
| 2020 | |
| Source Publication | ANALYTICAL CHEMISTRY
 |
| ISSN | 0003-2700 |
| Volume | 92Issue:3Pages:2770-2777 |
| Abstract | Proteomics emerges from the protein identification to protein functional elucidation, which depends to a large extent on the characterization of protein sequences. However, a large part of proteome sequences remains unannotated due to the limitation in proteolytic digestion by golden standard protease trypsin. Herein, we demonstrated that a cyanobacterial protease VAILase could specifically cleave at the short-chain aliphatic amino acids valine, alanine, leucine, isoleucine and threonine with cleavage specificity about 92% in total for proteomic analysis. The unique features of VAILase cleavage facilitate the characterization of most proteins and exhibit high complementarity to trypsin, and 22% of the covered sequences by VAILase are unique. VAILase can greatly improve the coverages of sequences with abundant aliphatic residues that are usually dark regions in conventional proteomic analysis, such as the transmembrane regions within anion exchanger 1 and photosystem II. |
| Subject Area | Chemistry, Analytical |
| DOI | 10.1021/acs.analchem.9b05048 |
| Indexed By | SCI |
| Language | 英语 |
| WOS Keyword | INTEGRAL MEMBRANE-PROTEINS ; EVOLVING PHOTOSYSTEM-II ; CRYSTAL-STRUCTURE ; HHOA PROTEASE ; TRYPSIN ; THROUGHPUT ; ACCURACIES ; BAND-3 |
| WOS Research Area | Chemistry |
| WOS ID | WOS:000511509400056 |
| Publisher | AMER CHEMICAL SOC |
| Subtype | Article |
| Publication Place | WASHINGTON |
| EISSN | 1520-6882 |
| Funding Organization | National Key R&D Program of China [2016YFF0200504] ; National Natural Science Foundation of ChinaNational Natural Science Foundation of China (NSFC) [91853101, 21675152] ; Original Innovation Project of CAS [ZDBSLY-SLH032] ; DICP [ZZBS201603] |
| Corresponding Author Email | wangfj@dicp.ac.cn |
| Citation statistics | |
| Document Type | 期刊论文 |
| Identifier | http://ir.ibcas.ac.cn/handle/2S10CLM1/21928 |
| Collection | 中科院光生物学重点实验室 |
| Affiliation | 1.Chinese Acad Sci, Dalian Inst Chem Phys, Dalian, Peoples R China 2.Univ Chinese Acad Sci, Beijing, Peoples R China 3.Chinese Acad Sci, Inst Bot, Beijing, Peoples R China 4.Chinese Acad Sci, Changchun Inst Appl Chem, Changchun, Peoples R China 5.Univ Sci & Technol China, Hefei, Peoples R China |
| Recommended Citation GB/T 7714 | Sun, Binwen,Liu, Zheyi,Fang, Zheng,et al. Probing the Proteomics Dark Regions by VAILase Cleavage at Aliphatic Amino Acids[J]. ANALYTICAL CHEMISTRY,2020,92(3):2770-2777. |
| APA | Sun, Binwen.,Liu, Zheyi.,Fang, Zheng.,Dong, Wei.,Yu, Yang.,...&Wang, Fangjun.(2020).Probing the Proteomics Dark Regions by VAILase Cleavage at Aliphatic Amino Acids.ANALYTICAL CHEMISTRY,92(3),2770-2777. |
| MLA | Sun, Binwen,et al."Probing the Proteomics Dark Regions by VAILase Cleavage at Aliphatic Amino Acids".ANALYTICAL CHEMISTRY 92.3(2020):2770-2777. |
| Files in This Item: | ||||||
| File Name/Size | DocType | Version | Access | License | ||
| S15206882_S152068822（2854KB） | 期刊论文 | 出版稿 | 开放获取 | CC BY-NC-SA | View Application Full Text | |
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