Proteomics

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Tailoring protein nanomechanics with chemical reactivity

ABSTRACT: The nanomechanical properties of elastomeric proteins determine the elasticity of a variety of tissues where modifications present at the covalent disulfide bonds can enhance protein stiffness. We propose an alternative chemical route to promote non-enzymatic oxidative protein folding via disulfide isomerization. Mass spectrometery has been used to determine the dynamics of S-thiolation and its role in modulating protein nanomechanics.

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Steven Lynham  

LAB HEAD: Sergi Garcia-Manyes

PROVIDER: PXD005981 | Pride | 2018-10-26

REPOSITORIES: pride

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File Name_ PR400_AB_CysNAC_2_moretryp.raw (F044875).mzid_File_Name__PR400_AB_CysNAC_2_moretryp.raw_(F044875).pride.mgf.gz Mzid
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File Name_ PR400_AB_Lcys_2_RR_newmethod.raw (F044824).mzid_File_Name__PR400_AB_Lcys_2_RR_newmethod.raw_(F044824).pride.mgf.gz Mzid
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Publications

Tailoring protein nanomechanics with chemical reactivity.

Beedle Amy E M AEM   Mora Marc M   Lynham Steven S   Stirnemann Guillaume G   Garcia-Manyes Sergi S  

Nature communications 20170606

The nanomechanical properties of elastomeric proteins determine the elasticity of a variety of tissues. A widespread natural tactic to regulate protein extensibility lies in the presence of covalent disulfide bonds, which significantly enhance protein stiffness. The prevalent in vivo strategy to form disulfide bonds requires the presence of dedicated enzymes. Here we propose an alternative chemical route to promote non-enzymatic oxidative protein folding via disulfide isomerization based on natu  ...[more]

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