Proteomics

Dataset Information

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Improvement of Peptide Separation for Exploring the Missing Proteins Localized on Membranes


ABSTRACT: How to separate hydrophobic peptides and to prevent loss of such peptides, nevertheless, have not been drawn enough attention (19). As a membrane protein possesses higher hydrophobicity, especially for one with multiple bilayer-exposed domains, efficient detection of hydrophobic peptides becomes a critical issue for its identification. It is generally recognized that MPs have two characteristics, relatively shorter sequences of amino acids and higher hydrophobicity.

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Placenta, Hela Cell

SUBMITTER: He Yanbin  

LAB HEAD: Siqi Liu

PROVIDER: PXD010630 | Pride | 2018-10-24

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
20180328_k562_mo_40frac_sub_1.raw Raw
20180328_k562_mo_40frac_sub_10.raw Raw
20180328_k562_mo_40frac_sub_11.raw Raw
20180328_k562_mo_40frac_sub_12.raw Raw
20180328_k562_mo_40frac_sub_13.raw Raw
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Publications

Improvement of Peptide Separation for Exploring the Missing Proteins Localized on Membranes.

Zhang Yuanliang Y   Lin Zhilong Z   Hao Piliang P   Hou Kexia K   Sui Yuanyuan Y   Zhang Keren K   He Yanbin Y   Li Hong H   Yang Huanming H   Liu Siqi S   Ren Yan Y  

Journal of proteome research 20181026 12


Following an enormous effort by the global scientific community coordinated by HUPO's Human Proteome Project, the number of proteins without high-quality MS or other evidence (colloquially termed missing proteins) has substantially decreased; however, some highly hydrophobic MPs remain on the list. We believe that efficient peptide separation is an approach that can be used to improve the identification of these hydrophobic MPs. We propose that peptides prepared from the membrane fractions of hu  ...[more]

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