Conformational flexibility of glycosylated peptides
| Autor: | Sören Doose, Markus Sauer, Lilly Nagel, Marc Löllmann, Norbert Sewald, Anne Burgert, Carolin Plattner, Stefan Bollmann |
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| Rok vydání: | 2011 |
| Předmět: |
Quantitative Biology::Biomolecules
Protein Folding Flexibility (anatomy) Glycosylation Chemistry Protein Conformation Protein dynamics Glycopeptides Fluorescence correlation spectroscopy Hydrogen Bonding Atomic and Molecular Physics and Optics Glycopeptide Mass Spectrometry Crystallography chemistry.chemical_compound medicine.anatomical_structure Oxazines medicine Computer Simulation Physical and Theoretical Chemistry Contact formation Chromatography High Pressure Liquid |
| Zdroj: | Chemphyschem : a European journal of chemical physics and physical chemistry. 12(16) |
| ISSN: | 1439-7641 |
| Popis: | With a twist: The conformational dynamics of glycosylated glycine–serine peptides is studied using contact- induced fluorescence quenching analysed by fluorescence correlation spectroscopy. End-to-end contact rates on ns–μs timescales reveal enthalpic and entropic contributions to the reduction of contact formation rates in glycopeptides (see picture). |
| Databáze: | OpenAIRE |
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