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Conformational Flexibility of Glycosylated Peptides
Author(s) -
Bollmann Stefan,
Burgert Anne,
Plattner Carolin,
Nagel Lilly,
Sewald Norbert,
Löllmann Marc,
Sauer Markus,
Doose Sören
Publication year - 2011
Publication title -
chemphyschem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.016
H-Index - 140
eISSN - 1439-7641
pISSN - 1439-4235
DOI - 10.1002/cphc.201100650
Subject(s) - chemistry , flexibility (engineering) , quenching (fluorescence) , glycine , twist , fluorescence spectroscopy , fluorescence , crystallography , amino acid , biochemistry , physics , mathematics , statistics , geometry , quantum mechanics
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).