Proteomics

Dataset Information

0

Peptide mapping of purified huntingtin protein samples from different eukaryotic expression systems


ABSTRACT: Huntingtin expression, purification and biophysical characterisation: purified huntingtin protein samples of different polyQ lengths derived from insect cell and mammalian cell production were digested and subject to peptide mass spectrometry.

INSTRUMENT(S): 6545 Q-TOF LC/MS

ORGANISM(S): Homo Sapiens (human) Spodoptera Frugiperda

TISSUE(S): Permanent Cell Line Cell

DISEASE(S): Huntington Disease

SUBMITTER: Suzanne Ackloo  

LAB HEAD: Cheryl H Arrowsmith

PROVIDER: PXD010865 | Pride | 2019-03-12

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
Cont-trypsin_Htt_HEK293_2.mgf Mgf
Cont-trypsin_Htt_HEK293_2.mzxml Mzxml
Cont-trypsin_Htt_HEK293_2.pep.xml Pepxml
Cont-trypsin_Htt_HEK293_2.pep.xml.zip Pepxml
Digesttest-22mingradientQ19HEK3195.mgf Mgf
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Publications

Design and characterization of mutant and wildtype huntingtin proteins produced from a toolkit of scalable eukaryotic expression systems.

Harding Rachel J RJ   Loppnau Peter P   Ackloo Suzanne S   Lemak Alexander A   Hutchinson Ashley A   Hunt Brittany B   Holehouse Alex S AS   Ho Jolene C JC   Fan Lixin L   Toledo-Sherman Leticia L   Seitova Alma A   Arrowsmith Cheryl H CH  

The Journal of biological chemistry 20190306 17


The gene mutated in individuals with Huntington's disease (HD) encodes the 348-kDa huntingtin (HTT) protein. Pathogenic HD CAG-expansion mutations create a polyglutamine (polyQ) tract at the N terminus of HTT that expands above a critical threshold of ∼35 glutamine residues. The effect of these HD mutations on HTT is not well understood, in part because it is difficult to carry out biochemical, biophysical, and structural studies of this large protein. To facilitate such studies, here we have ge  ...[more]

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