Roberto F. Delgadillo, Ph.D.

Affiliations: 
2009 Chemistry The University of Nebraska - Lincoln, Lincoln, NE 
 2016-2010 Instituto Tecnologico y de Estudios Superiores de Monterrey (Mexico) 
Area:
General Chemistry
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"Roberto Delgadillo"
Bio:

https://www.researchgate.net/profile/Roberto-Delgadillo

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Parents

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Lawrence J. Parkhurst grad student 2009 University of Nebraska - Lincoln
 (Acceptor detected fluorescence resonance energy transfer for measurement up to 250 A and biophysical studies on core TATA binding protein-DNA complex.)
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Publications

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Delgadillo RF, Carnes KA, Zaleta-Rivera K, et al. (2021) A FLIM Microscopy Based on Acceptor-Detected Förster Resonance Energy Transfer. Analytical Chemistry
Delgadillo RF, Carnes KA, Valles-Villarreal N, et al. (2020) Dual-Channel Stopped-Flow Apparatus for Simultaneous Fluorescence, Anisotropy, and FRET Kinetic Data Acquisition for Binary and Ternary Biological Complexes. Biosensors. 10
Delgadillo RF, Mueser TC, Zaleta-Rivera K, et al. (2019) Detailed characterization of the solution kinetics and thermodynamics of biotin, biocytin and HABA binding to avidin and streptavidin. Plos One. 14: e0204194
Delgadillo RF, Parker ML, Lebrun M, et al. (2016) Stability of the Plasmodium falciparum AMA1-RON2 Complex Is Governed by the Domain II (DII) Loop. Plos One. 11: e0144764
Delgadillo RF, Lebrun M, Boulanger M, et al. (2015) Kinetics and Thermodynamics of Apicomplexa AMA1-RON2Sp Interaction Biophysical Journal. 108: 344a
Delgadillo RF, Parkhurst LJ, Mueser TC, et al. (2012) Kinetics of Biotin Derivatives Binding to Avidin and Streptavidin Biophysical Journal. 102: 217a
Delgadillo RF, Parkhurst LJ. (2010) Spectroscopic properties of fluorescein and rhodamine dyes attached to DNA. Photochemistry and Photobiology. 86: 261-72
Delgadillo RF, Whittington JE, Parkhurst LK, et al. (2009) The TATA-binding protein core domain in solution variably bends TATA sequences via a three-step binding mechanism. Biochemistry. 48: 1801-9
Whittington JE, Delgadillo RF, Attebury TJ, et al. (2008) TATA-binding protein recognition and bending of a consensus promoter are protein species dependent. Biochemistry. 47: 7264-73
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