Analysis of Protein–DNA Interactions Using Surface Plasmon Resonance and a ReDCaT Chip

2021 ◽  
pp. 369-379
Author(s):  
Clare E. M. Stevenson ◽  
David M. Lawson
Keyword(s):  
Surface Plasmon Resonance ◽  
Surface Plasmon ◽  
Plasmon Resonance ◽  
Dna Interactions ◽  
Protein Dna Interactions

SURFACE PLASMON RESONANCE SPECTROSCOPY AND QUARTZ CRYSTAL MICROBALANCE STUDY OF PROTEIN-DNA INTERACTIONS IN HORMONE RECEPTOR BIOLOGY

COSMOS ◽  
2009 ◽  
Vol 05 (01) ◽  
pp. 79-95
Author(s):  
XIAODI SU
Keyword(s):  
Surface Plasmon Resonance ◽  
Surface Plasmon ◽  
Quartz Crystal Microbalance ◽  
Conformational Changes ◽  
Plasmon Resonance ◽  
Quartz Crystal ◽  
Resonance Spectroscopy ◽  
Dna Interactions ◽  
Protein Dna Interactions

Surface plasmon resonance (SPR) spectroscopy and quartz crystal microbalance (QCM) are surface sensitive analytical techniques capable of real-time monitoring of biomolecular interactions. In this article we review our past work on the use of these two techniques for studying protein–DNA interactions, exemplified with estrogen receptors (ER) and their response elements (ERE). Various assay schemes have been developed for a comprehensive characterization of ER–ERE interactions in terms of sequence specificity, binding affinity, stoichiometry, ligand effects on binding dynamics and conformational changes in the proteins and DNA. These are all important characteristics underlining the mechanism of ER-mediated gene transcription. With these studies we have made the following demonstrations to describe the advantages of these two techniques, namely (i) SPR technique is superior and more versatile than conventional (electrophoretic mobility shift assay) EMSA for studying protein-DNA interactions; (ii) QCM is an alternative tool for studying conformational changes in protein–DNA complexes and (iii) combinational SPR and QCM analysis provides additional characterization of biomolecular films, e.g. film thickness, water content, and conformation rigidity etc.

Semiquantitative and quantitative analysis of protein–DNA interactions using steady-state measurements in surface plasmon resonance competition experiments

2013 ◽  
Vol 440 (2) ◽  
pp. 178-185 ◽  
Author(s):  
Roland Gamsjaeger ◽  
Ruvini Kariawasam ◽  
Line H. Bang ◽  
Christine Touma ◽  
Cuong D. Nguyen ◽  
...  
Keyword(s):  
Surface Plasmon Resonance ◽  
Steady State ◽  
Quantitative Analysis ◽  
Surface Plasmon ◽  
Plasmon Resonance ◽  
Dna Interactions ◽  
Protein Dna Interactions

Dendrimer functionalization of gold surface improves the measurement of protein–DNA interactions by surface plasmon resonance imaging

2013 ◽  
Vol 43 ◽  
pp. 148-154 ◽  
Author(s):  
Flavien Pillet ◽  
Aurore Sanchez ◽  
Cécile Formosa ◽  
Marjorie Séverac ◽  
Emmanuelle Trévisiol ◽  
...  
Keyword(s):  
Surface Plasmon Resonance ◽  
Surface Plasmon ◽  
Plasmon Resonance ◽  
Gold Surface ◽  
Surface Plasmon Resonance Imaging ◽  
Resonance Imaging ◽  
Dna Interactions ◽  
Protein Dna Interactions

Probing protein: DNA interactions using a uniform monolayer of DNA and surface plasmon resonance

2000 ◽  
Author(s):  
Jennifer S. Shumaker-Parry ◽  
Charles T. Campbell ◽  
Gary D. Stormo ◽  
Fauzi S. Silbaq ◽  
Rudolf H. Aebersold
Keyword(s):  
Surface Plasmon Resonance ◽  
Surface Plasmon ◽  
Plasmon Resonance ◽  
Dna Interactions ◽  
Protein Dna Interactions

scholarly journals Real-Time Analysis of Specific Protein-DNA Interactions with Surface Plasmon Resonance

2012 ◽  
Vol 2012 ◽  
pp. 1-19 ◽  
Author(s):  
Markus Ritzefeld ◽  
Norbert Sewald
Keyword(s):  
Surface Plasmon Resonance ◽  
Real Time ◽  
Surface Plasmon ◽  
Dna Sequences ◽  
Plasmon Resonance ◽  
Interaction Analysis ◽  
Physical Phenomenon ◽  
Dna Interactions ◽  
Protein Dna Interactions ◽  
Rna Interaction

Several proteins, like transcription factors, bind to certain DNA sequences, thereby regulating biochemical pathways that determine the fate of the corresponding cell. Due to these key positions, it is indispensable to analyze protein-DNA interactions and to identify their mode of action. Surface plasmon resonance is a label-free method that facilitates the elucidation of real-time kinetics of biomolecular interactions. In this article, we focus on this biosensor-based method and provide a detailed guide how SPR can be utilized to study binding of proteins to oligonucleotides. After a description of the physical phenomenon and the instrumental realization including fiber-optic-based SPR and SPR imaging, we will continue with a survey of immobilization methods. Subsequently, we will focus on the optimization of the experiment, expose pitfalls, and introduce how data should be analyzed and published. Finally, we summarize several interesting publications of the last decades dealing with protein-DNA and RNA interaction analysis by SPR.

Sign in / Sign up

Export Citation Format

Share Document