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Polyglutamine Aggregation Nucleation: Thermodynamics of a Highly Unfavorable Protein Folding Reactio...

Polyglutamine Aggregation Nucleation: Thermodynamics of a Highly Unfavorable Protein Folding Reactio...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_journals_201356551

Polyglutamine Aggregation Nucleation: Thermodynamics of a Highly Unfavorable Protein Folding Reaction

About this item

Full title

Polyglutamine Aggregation Nucleation: Thermodynamics of a Highly Unfavorable Protein Folding Reaction

Publisher

United States: National Academy of Sciences

Journal title

Proceedings of the National Academy of Sciences - PNAS, 2005-10, Vol.102 (43), p.15400-15405

Language

English

Formats

Publication information

Publisher

United States: National Academy of Sciences

More information

Scope and Contents

Contents

Polyglutamine (polyGln) aggregation is implicated in the disease progression of Huntington's disease and other expanded CAG repeat diseases. PolyGIn aggregation in vitro follows a simple nucleated growth polymerization pathway without apparent complications such as populated intermediates, alternative assembly pathways, or secondary nucleation phen...

Alternative Titles

Full title

Polyglutamine Aggregation Nucleation: Thermodynamics of a Highly Unfavorable Protein Folding Reaction

Authors, Artists and Contributors

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_proquest_journals_201356551

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_journals_201356551

Other Identifiers

ISSN

0027-8424

E-ISSN

1091-6490

DOI

10.1073/pnas.0501651102

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