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
Zeitschriftennummer
16
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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.

Förster resonance energy transfer and protein-induced fluorescence enhancement as synergetic multi-scale molecular rulers.
Ploetz E, Lerner E, Husada F, Roelfs M, Chung S, Hohlbein J, Weiss S, Cordes T., Sci Rep 6(), 2016
PMID: 27641327
The roughness of the protein energy landscape results in anomalous diffusion of the polypeptide backbone.
Volk M, Milanesi L, Waltho JP, Hunter CA, Beddard GS., Phys Chem Chem Phys 17(2), 2015
PMID: 25412176
Photophysical processes in single molecule organic fluorescent probes.
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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