scholarly journals Combining Bottom-Up and Top-Down Mass Spectrometric Strategies for De Novo Sequencing of the Crustacean Hyperglycemic Hormone from Cancer borealis

2009 ◽  
Vol 81 (1) ◽  
pp. 240-247 ◽  
Author(s):  
Mingming Ma ◽  
Ruibing Chen ◽  
Ying Ge ◽  
Huan He ◽  
Alan G. Marshall ◽  
...  
PROTEOMICS ◽  
2017 ◽  
Vol 17 (23-24) ◽  
pp. 1600321 ◽  
Author(s):  
Kira Vyatkina ◽  
Lennard J. M. Dekker ◽  
Si Wu ◽  
Martijn M. VanDuijn ◽  
Xiaowen Liu ◽  
...  

2021 ◽  
Vol 22 (11) ◽  
pp. 5476
Author(s):  
Bing Wang ◽  
Zhiwei Wang ◽  
Ni Pan ◽  
Jiangmei Huang ◽  
Cuihong Wan

Small open reading frames (sORFs) have translational potential to produce peptides that play essential roles in various biological processes. Nevertheless, many sORF-encoded peptides (SEPs) are still on the prediction level. Here, we construct a strategy to analyze SEPs by combining top-down and de novo sequencing to improve SEP identification and sequence coverage. With de novo sequencing, we identified 1682 peptides mapping to 2544 human sORFs, which were all first characterized in this work. Two-thirds of these new sORFs have reading frame shifts and use a non-ATG start codon. The top-down approach identified 241 human SEPs, with high sequence coverage. The average length of the peptides from the bottom-up database search was 19 amino acids (AA); from de novo sequencing, it was 9 AA; and from the top-down approach, it was 25 AA. The longer peptide positively boosts the sequence coverage, more efficiently distinguishing SEPs from the known gene coding sequence. Top-down has the advantage of identifying peptides with sequential K/R or high K/R content, which is unfavorable in the bottom-up approach. Our method can explore new coding sORFs and obtain highly accurate sequences of their SEPs, which can also benefit future function research.


2015 ◽  
Vol 14 (11) ◽  
pp. 4450-4462 ◽  
Author(s):  
Kira Vyatkina ◽  
Si Wu ◽  
Lennard J. M. Dekker ◽  
Martijn M. VanDuijn ◽  
Xiaowen Liu ◽  
...  

2007 ◽  
Vol 79 (16) ◽  
pp. 6236-6248 ◽  
Author(s):  
Leesa J. Deterding ◽  
Suchandra Bhattacharjee ◽  
Dario C. Ramirez ◽  
Ronald P. Mason ◽  
Kenneth B. Tomer

2005 ◽  
Vol 77 (22) ◽  
pp. 7163-7171 ◽  
Author(s):  
Michael J. Chalmers ◽  
Colin Logan Mackay ◽  
Christopher L. Hendrickson ◽  
Stefan Wittke ◽  
Michael Walden ◽  
...  

2015 ◽  
Vol 26 (3) ◽  
pp. 482-492 ◽  
Author(s):  
Yelena Yefremova ◽  
Mahmoud Al-Majdoub ◽  
Kwabena F. M. Opuni ◽  
Cornelia Koy ◽  
Weidong Cui ◽  
...  

2002 ◽  
Vol 1 (3) ◽  
pp. 239-252 ◽  
Author(s):  
Nathan C. VerBerkmoes ◽  
Jonathan L. Bundy ◽  
Loren Hauser ◽  
Keiji G. Asano ◽  
Jane Razumovskaya ◽  
...  

2018 ◽  
Vol 1 (1) ◽  
pp. e00005 ◽  
Author(s):  
K.V. Vyatkina

Determination of the primary structure of proteins and peptides constitutes an important step in studying their properties. Currently, mass spectrometry is commonly applied to this end. The results of mass spectrometric measurements can be interpreted by means of either a database search or de novo sequencing methods. The appeal of the latter is due to their applicability to investigating unknown proteins, as well as the ones that cannot be analyzed with genomics or transcriptomics methods. In this paper, we briefly review the existing approaches to de novo sequencing of proteins and peptides, along with the problems that can be solved using those, and indicate directions and perspectives for their further development.


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