Conformational Flexibility of Glycosylated Peptides

Bollmann S, Burgert A, Plattner C, Nagel L, Sewald N, Löllmann M, Sauer M, Doose S (2011)
ChemPhysChem 12(16): 2907-2911.

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Zeitschriftenaufsatz | Veröffentlicht | Englisch
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Abstract / Bemerkung
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).
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Zeitschriftentitel
ChemPhysChem
Band
12
Ausgabe
16
Seite(n)
2907-2911
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Bollmann S, Burgert A, Plattner C, et al. Conformational Flexibility of Glycosylated Peptides. ChemPhysChem. 2011;12(16):2907-2911.
Bollmann, S., Burgert, A., Plattner, C., Nagel, L., Sewald, N., Löllmann, M., Sauer, M., et al. (2011). Conformational Flexibility of Glycosylated Peptides. ChemPhysChem, 12(16), 2907-2911. doi:10.1002/cphc.201100650
Bollmann, S., Burgert, A., Plattner, C., Nagel, L., Sewald, N., Löllmann, M., Sauer, M., and Doose, S. (2011). Conformational Flexibility of Glycosylated Peptides. ChemPhysChem 12, 2907-2911.
Bollmann, S., et al., 2011. Conformational Flexibility of Glycosylated Peptides. ChemPhysChem, 12(16), p 2907-2911.
S. Bollmann, et al., “Conformational Flexibility of Glycosylated Peptides”, ChemPhysChem, vol. 12, 2011, pp. 2907-2911.
Bollmann, S., Burgert, A., Plattner, C., Nagel, L., Sewald, N., Löllmann, M., Sauer, M., Doose, S.: Conformational Flexibility of Glycosylated Peptides. ChemPhysChem. 12, 2907-2911 (2011).
Bollmann, Stefan, Burgert, Anne, Plattner, Carolin, Nagel, Lilly, Sewald, Norbert, Löllmann, Marc, Sauer, Markus, and Doose, Sören. “Conformational Flexibility of Glycosylated Peptides”. ChemPhysChem 12.16 (2011): 2907-2911.

4 Zitationen in Europe PMC

Daten bereitgestellt von Europe PubMed Central.

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Ploetz E, Lerner E, Husada F, Roelfs M, Chung S, Hohlbein J, Weiss S, Cordes T., Sci Rep 6(), 2016
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The roughness of the protein energy landscape results in anomalous diffusion of the polypeptide backbone.
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Stennett EM, Ciuba MA, Levitus M., Chem Soc Rev 43(4), 2014
PMID: 24141280
Systematic evaluation of fluorescence correlation spectroscopy data analysis on the nanosecond time scale.
Steger K, Bollmann S, Noé F, Doose S., Phys Chem Chem Phys 15(25), 2013
PMID: 23685745

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