Conformational Flexibility of Glycosylated Peptides
Journal article published in 2011 by
Stefan Bollmann,
Anne Burgert,
Carolin Plattner,
Lilly Nagel,
Norbert Sewald,
Marc Löllmann,
Markus Sauer,
Sören Doose 
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Abstract
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).