Otto, C.

( C. Otto)

protein molecule uorescence binding egfpxpa substrate interaction confocal solution bubble concentration nucleotide excision repair repair uorescent scanning complex image sample result water 3.5 emission study microscopy fluorescence buffer detection fraction method excision diffusion trace presence excitation agarose ﬂ uorescent proteins spectroscopy correlation reaction dynamic activity cy 3.5bubble dna nucleotide acids research bubble dna surfactant measurement molecule level surface analysis damage figure cy 3.5 autocorrelation channel mechanism egfpxpa molecules experiment cy 3.5 emission dsdna volume number column residence times dna substrates functionality ﬂ uorescent protein region position replication protein egfp emission emission detection time trace hoeijmaker uorescence behavior dna molecules level tx 100 uorescent protein function

3 Most Recent Publications

Quantitative fluorescence correlation spectroscopy reveals a 1000-fold increase in lifetime of protein functionality (Article) Zhang, D. Lans, W.J. Vermeulen, W. Lenferink, A. Otto, C.	2008-10-01
Fluorescence correlation spectroscopy of the binding of nucleotide excision repair protein XPC-hHr23B with DNA substrates (Article) Roche, Y. Zhang, D. Segers-Nolten, G.M. Vermeulen, W. Wyman, C. Sugasawa, K. Hoeijmakers, J.H.J. Otto, C.	2008-09-01
Scanning confocal fluorescence microscopy for single molecule analysis of nucleotide excision repair complexes. (Article) Segers-Nolten, G.M. Wyman, C. Wijgers, N. Vermeulen, W. Lenferink, A.T. Hoeijmakers, J.H.J. Greve, J. Otto, C.	2002-01-01

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