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MetabolomicsNew plasma preparation approach to enrich metabolome coverage in untargeted metabolomics: plasma protein bound hydrophobic metabolite release with proteinase K
Plasma untargeted metabolomics is a common method for evaluation of the mechanisms underlying human pathologies and identification of novel biomarkers. The plasma proteins provide the environment for transport of hydrophobic metabolites. The current sample preparation protocol relies on the immediat...
2022-03-18 | MTBLS670 | MetaboLights
MetabolomicsProteome allocations change linearly with the specific growth rate of Saccharomyces cerevisiae under glucose limitation

Saccharomyces cerevisiae is a widely used cell factory; therefore, it is important to understand how it organizes key functional parts when cultured under different conditions. Here, we perform a multiomics analysis of S. cerevisiae by culturing the strain with a wide range of s...

2022-08-31 | MTBLS697 | MetaboLights
ProteomicsCleavable Hydrophobic Derivatization Strategy for Enrichment and Identification of Phosphorylated Lysine Peptides
Herein, a cleavable hydrophobic derivatization (CHD) strategy was established for the enrichment and identification of pLys peptides. By CHD, 2,5-dioxopyrrolidin-1-yl-3-(decyldisulfanyl)propanoate (Dec-disulf-NHS) was synthesized to react with lysine dephosphorylated peptides, and then the derived p...
ORGANISM(S): Escherichia Coli 
2019-02-12 | PXD012682 |
UnknownExploring the dark foldable proteome by considering hydrophobic amino acids topology.
Not available
S-EPMC5278394 | biostudies-literature
ProteomicsHydrophobic interaction chromatography for bottom-up proteomics
Hydrophobic interaction chromatography as a first dimension to reduce samples complexity for bottom-up proteomics analyses of single proteins and protein complexes
ORGANISM(S): Homo sapiens (Human) 
2017-05-16 | PXD006217 | Pride
Lc-ms/ms  hic  human 
ProteomicsChemical-proteomics profiling of reactive cysteines near a hydrophobic pocket
This project investigates reactive cysteine residues located near hydrophobic pockets in proteins, features conserved in autopalmitoylated proteins. S-palmitoylation is a post-translational modification that regulates protein localization and function, and has been implicated in neurological, metabo...
ORGANISM(S): Homo sapiens (Human) 
2025-11-20 | PXD070770 | Pride
Autopalmitoylation Hydrophobic pockets Chemical proteomics Reactive cysteines Druggable sites 
ProteomicsHydrophobic tagging-assisted N-termini enrichment (HYTANE) for in-depth N-terminome analysis
The analysis of protein N-termini is of great importance for understanding the protein function and elucidating the proteolytic processing. Herein, we develop a negative enrichment strategy, termed as hydrophobic tagging-assisted N-termini enrichment (HYTANE) to achieve a global N-terminome analysis...
ORGANISM(S): Homo sapiens (Human) Saccharomyces cerevisiae (Baker's yeast) 
2016-08-19 | PXD004690 | Pride
Sacchoromyces cerevisiae Jurkat N-termini Caspase 
Proteomicsn-Dodecyl-β-D-maltopyranoside (DDM)-Assisted Resolubilization Enhances Hydrophobic Peptide and Protein Identification in Bottom-Up Proteomics
This study demonstrates that adding the non-ionic surfactant n-dodecyl-β-D-maltopyranoside (DDM) during protein resolubilization improves the identification of hydrophobic peptides and proteins in bottom-up proteomics. DDM's effectiveness in overcoming the challenge of losing hydrophobic proteins af...
ORGANISM(S): Mus musculus (Mouse) 
2025-12-16 | PXD064279 | Pride
Macrophages Protein resolubilization Immunoproteomics N-dodecyl-β-d-maltopyranoside (ddm) Hydrophobic proteome S-palmitoylation 
UnknownMALDI/MS peptide mass fingerprinting for proteome analysis: identification of hydrophobic proteins attached to eucaryote keratinocyte cytoplasmic membrane using different matrices in concert.
Not available
S-EPMC156602 | biostudies-literature
UnknownAtomic insights into the effects of pathological mutants through the disruption of hydrophobic core in the prion protein.
Not available
S-EPMC6915724 | biostudies-literature
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