Journal article
Kinetics of the self-aggregation and film formation of poly-L-proline at high temperatures explored by circular dichroism spectroscopy
Biopolymers, Vol.93(5), pp.451-457
May 2010
PMID: 19998404
Abstract
Poly-L-proline has been used as a model system for various purposes over a period of more than 60 years. Its relevance among the protein/peptide community stems from its use as a reference system for determining the conformational distributions of unfolded peptides and proteins, its use as a molecular ruler, and from the pivotal role of proline residues in conformational transitions and protein-protein interactions. While several studies indicate that polyproline can aggregate and precipitate in aqueous solution, a systematic study of the aggregation process is still outstanding. We found, by means of UV-circular dichroism and IR measurements, that polyproline is predominantly monomeric at room temperature at millimolar concentrations. Upon heating, the polypeptide stays in its monomeric state until the temperature reaches a threshold of ca. 60 degrees C. At higher temperatures, the peptide aggregates as a film on the inside surface of the employed cuvette. The process proceeds on a time scale of 10(3) s and can best be described by a bi-exponential relaxation function. The respective CD and IR spectra are qualitatively different from the canonical spectra of polyproline in aqueous solution, and are indicative of a highly packed state.
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Details
- Title
- Kinetics of the self-aggregation and film formation of poly-L-proline at high temperatures explored by circular dichroism spectroscopy
- Creators
- Lonna Tooke - Department of Chemistry, Drexel University, Philadelphia, PA 19104, USALaura DuitchThomas J MeaseyReinhard Schweitzer-Stenner
- Publication Details
- Biopolymers, Vol.93(5), pp.451-457
- Publisher
- Wiley; United States
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Chemistry
- Identifiers
- 991014877957604721
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- Web of Science research areas
- Biochemistry & Molecular Biology
- Biophysics