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.

Zeitschriftenaufsatz | Veröffentlicht | Englisch
 
Download
Es wurden keine Dateien hochgeladen. Nur Publikationsnachweis!
DOI
Autor*in
Bollmann, Stefan; Burgert, Anne; Plattner, Carolin; Nagel, LillyUniBi; Sewald, NorbertUniBi ; Löllmann, Marc; Sauer, Markus; Doose, Sören
Einrichtung
Fakultät für Chemie > Organische Chemie III
Centrum für Biotechnologie > Arbeitsgruppe N. Sewald
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).
Erscheinungsjahr
2011
Zeitschriftentitel
ChemPhysChem
Band
12
Ausgabe
16
Seite(n)
2907-2911
ISSN
1439-4235
Page URI
https://pub.uni-bielefeld.de/record/2447685

Zitieren

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, Stefan, Burgert, Anne, Plattner, Carolin, Nagel, Lilly, Sewald, Norbert, Löllmann, Marc, Sauer, Markus, and Doose, Sören. 2011. “Conformational Flexibility of Glycosylated Peptides”. ChemPhysChem 12 (16): 2907-2911.
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

36 References

Daten bereitgestellt von Europe PubMed Central.


Gabius, 2009
Lectins: Carbohydrate-Specific Proteins That Mediate Cellular Recognition.
Lis H, Sharon N., Chem. Rev. 98(2), 1998
PMID: 11848911

AUTHOR UNKNOWN, 0
N-linked oligosaccharides as outfitters for glycoprotein folding, form and function.
Mitra N, Sinha S, Ramya TN, Surolia A., Trends Biochem. Sci. 31(3), 2006
PMID: 16473013
Folding of glycoproteins: toward understanding the biophysics of the glycosylation code.
Shental-Bechor D, Levy Y., Curr. Opin. Struct. Biol. 19(5), 2009
PMID: 19647993

Imperiali, Acc. Chem. Res. 30(), 1997

Tachibana, Angew. Chem. 116(), 2004
Antifreeze glycoproteins: elucidation of the structural motifs that are essential for antifreeze activity.
Tachibana Y, Fletcher GL, Fujitani N, Tsuda S, Monde K, Nishimura S., Angew. Chem. Int. Ed. Engl. 43(7), 2004
PMID: 14767958
Conformational studies of oligosaccharides and glycopeptides: complementarity of NMR, X-ray crystallography, and molecular modelling.
Wormald MR, Petrescu AJ, Pao YL, Glithero A, Elliott T, Dwek RA., Chem. Rev. 102(2), 2002
PMID: 11841247
Mucin biophysics.
Bansil R, Stanley E, LaMont JT., Annu. Rev. Physiol. 57(), 1995
PMID: 7778881
Effect of N-linked glycosylation on glycopeptide and glycoprotein structure.
Imperiali B, O'Connor SE., Curr Opin Chem Biol 3(6), 1999
PMID: 10600722

AUTHOR UNKNOWN, 0
Biological and chemical applications of fluorescence correlation spectroscopy: a review.
Hess ST, Huang S, Heikal AA, Webb WW., Biochemistry 41(3), 2002
PMID: 11790090
Fluorescence correlation spectroscopy. II. An experimental realization.
Magde D, Elson EL, Webb WW., Biopolymers 13(1), 1974
PMID: 4818131

AUTHOR UNKNOWN, 0
Fluorescence quenching by photoinduced electron transfer: a reporter for conformational dynamics of macromolecules.
Doose S, Neuweiler H, Sauer M., Chemphyschem 10(9-10), 2009
PMID: 19475638
A close look at fluorescence quenching of organic dyes by tryptophan.
Doose S, Neuweiler H, Sauer M., Chemphyschem 6(11), 2005
PMID: 16224752
A microscopic view of miniprotein folding: enhanced folding efficiency through formation of an intermediate.
Neuweiler H, Doose S, Sauer M., Proc. Natl. Acad. Sci. U.S.A. 102(46), 2005
PMID: 16269542
Dynamics of unfolded polypeptide chains in crowded environment studied by fluorescence correlation spectroscopy.
Neuweiler H, Lollmann M, Doose S, Sauer M., J. Mol. Biol. 365(3), 2006
PMID: 17084857
Probing polyproline structure and dynamics by photoinduced electron transfer provides evidence for deviations from a regular polyproline type II helix.
Doose S, Neuweiler H, Barsch H, Sauer M., Proc. Natl. Acad. Sci. U.S.A. 104(44), 2007
PMID: 17956989
Using photoinduced charge transfer reactions to study conformational dynamics of biopolymers at the single-molecule level.
Neuweiler H, Sauer M., Curr Pharm Biotechnol 5(3), 2004
PMID: 15180550
The initial step of DNA hairpin folding: a kinetic analysis using fluorescence correlation spectroscopy.
Kim J, Doose S, Neuweiler H, Sauer M., Nucleic Acids Res. 34(9), 2006
PMID: 16687657

Lakowicz, 1999
Hydrogen-bond driven loop-closure kinetics in unfolded polypeptide chains.
Daidone I, Neuweiler H, Doose S, Sauer M, Smith JC., PLoS Comput. Biol. 6(1), 2010
PMID: 20098498
Molecular basis for the effect of urea and guanidinium chloride on the dynamics of unfolded polypeptide chains.
Moglich A, Krieger F, Kiefhaber T., J. Mol. Biol. 345(1), 2005
PMID: 15567418
Solvent viscosity and friction in protein folding dynamics.
Hagen SJ., Curr. Protein Pept. Sci. 11(5), 2010
PMID: 20426733

Kramers, Physica 7(), 1940

Szabo, J. Chem. Phys. 72(), 1980
Effect of glycosylation on protein folding: a close look at thermodynamic stabilization.
Shental-Bechor D, Levy Y., Proc. Natl. Acad. Sci. U.S.A. 105(24), 2008
PMID: 18550810

AUTHOR UNKNOWN, 0
Backbone-driven collapse in unfolded protein chains.
Teufel DP, Johnson CM, Lum JK, Neuweiler H., J. Mol. Biol. 409(2), 2011
PMID: 21497607
End-to-end distance distributions and intrachain diffusion constants in unfolded polypeptide chains indicate intramolecular hydrogen bond formation.
Moglich A, Joder K, Kiefhaber T., Proc. Natl. Acad. Sci. U.S.A. 103(33), 2006
PMID: 16894178

AUTHOR UNKNOWN, 0
The effect of glycosylation on interparticle interactions and dimensions of native and denatured phytase.
Hoiberg-Nielsen R, Westh P, Arleth L., Biophys. J. 96(1), 2009
PMID: 18835893
Role of glycosylation on the conformation and chain dimensions of O-linked glycoproteins: light-scattering studies of ovine submaxillary mucin.
Shogren R, Gerken TA, Jentoft N., Biochemistry 28(13), 1989
PMID: 2775721

Mathlouthi, 1995
Material in PUB:
Teil dieser Dissertation
Synthese und Charakterisierung von modifizierten Antigefrierglykopeptiden
Nagel L (2012)
Bielefeld.
Export

Markieren/ Markierung löschen
Markierte Publikationen

Open Data PUB

Web of Science

Dieser Datensatz im Web of Science®
Quellen

PMID: 21922630
PubMed | Europe PMC

Suchen in

Google Scholar