Proteomics

Dataset Information

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LC-MSMS of Hela cell extracts on pull down with de novo modular peptide binding proteins


ABSTRACT: we describe a general approach for de novo design of proteins made out of repeating units that bind peptides with repeating sequences such that there is a one to one correspondence between repeat units on the protein and peptide. We develop a rapid docking plus geometric hashing method to identify protein backbones and protein-peptide rigid body arrangements that are compatible with bidentate hydrogen bonds between side chains on the protein and the backbone of the peptide; the remainder of the protein sequence is then designed using Rosetta to incorporate additional interactions with the peptide and drive folding to the desired structure. We use this approach to design, from scratch, alpha helical repeat proteins that bind six different tripeptide repeat sequences--PLP, LRP, PEW, IYP, PRM and PKW-- in near polyproline 2 helical conformations.

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Hela Cell

SUBMITTER: Tomos Morgan  

LAB HEAD: Emmanuel Derivery

PROVIDER: PXD038492 | Pride | 2023-03-17

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
0_1.raw Raw
0_1.raw__F171018_.mzid.gz Mzid
0_1.raw__F171018_.mzid_0_1.raw__F171018_.MGF Mzid
0_2.raw Raw
0_2.raw__F171019_.mzid.gz Mzid
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Publications


General approaches for designing sequence-specific peptide-binding proteins would have wide utility in proteomics and synthetic biology. However, designing peptide-binding proteins is challenging, as most peptides do not have defined structures in isolation, and hydrogen bonds must be made to the buried polar groups in the peptide backbone<sup>1-3</sup>. Here, inspired by natural and re-engineered protein-peptide systems<sup>4-11</sup>, we set out to design proteins made out of repeating units t  ...[more]

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