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DNA-Protein Interactions

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Cover of 'DNA-Protein Interactions'

Table of Contents

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    Book Overview
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    Chapter 1 Electrophoretic Mobility Shift Assay Using Radiolabeled DNA Probes
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    Chapter 2 In Vitro DNase I Footprinting
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    Chapter 3 DNA-Protein Interactions
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    Chapter 4 In Cellulo DNA Analysis: LMPCR Footprinting.
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    Chapter 5 Southwestern Blotting Assay
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    Chapter 6 Single-Molecule Approaches for the Characterization of Riboswitch Folding Mechanisms
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    Chapter 7 Probing of Nascent Riboswitch Transcripts
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    Chapter 8 DNA-Protein Interactions
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    Chapter 9 Precise Identification of Genome-Wide Transcription Start Sites in Bacteria by 5'-Rapid Amplification of cDNA Ends (5'-RACE).
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    Chapter 10 Analysis of DNA Supercoiling Induced by DNA-Protein Interactions.
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    Chapter 11 Precise Identification of DNA-Binding Proteins Genomic Location by Exonuclease Coupled Chromatin Immunoprecipitation (ChIP-exo).
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    Chapter 12 The Cruciform DNA Mobility Shift Assay: A Tool to Study Proteins That Recognize Bent DNA.
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    Chapter 13 Individual and Sequential Chromatin Immunoprecipitation Protocols.
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    Chapter 14 Chromatin Endogenous Cleavage (ChEC) as a Method to Quantify Protein Interaction with Genomic DNA in Saccharomyces cerevisiae.
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    Chapter 15 Selection and Validation of Spacer Sequences for CRISPR-Cas9 Genome Editing and Transcription Regulation in Bacteria.
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    Chapter 16 Detection of Short-Range DNA Interactions in Mammalian Cells Using High-Resolution Circular Chromosome Conformation Capture Coupled to Deep Sequencing.
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    Chapter 17 Global Mapping of Open Chromatin Regulatory Elements by Formaldehyde-Assisted Isolation of Regulatory Elements Followed by Sequencing (FAIRE-seq).
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    Chapter 18 Aggregate and Heatmap Representations of Genome-Wide Localization Data Using VAP, a Versatile Aggregate Profiler.
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    Chapter 19 Circular Dichroism for the Analysis of Protein–DNA Interactions
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    Chapter 20 Quantitative Investigation of Protein–Nucleic Acid Interactions by Biosensor Surface Plasmon Resonance
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    Chapter 21 Identification of Nucleic Acid High Affinity Binding Sequences of Proteins by SELEX
Attention for Chapter 20: Quantitative Investigation of Protein–Nucleic Acid Interactions by Biosensor Surface Plasmon Resonance
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Chapter title
Quantitative Investigation of Protein–Nucleic Acid Interactions by Biosensor Surface Plasmon Resonance
Chapter number 20
Book title
DNA-Protein Interactions
Published in
Methods in molecular biology, January 2015
DOI 10.1007/978-1-4939-2877-4_20
Pubmed ID
Book ISBNs
978-1-4939-2876-7, 978-1-4939-2877-4
Authors

Shuo Wang, Gregory M. K. Poon, W. David Wilson, Wang, Shuo, Poon, Gregory M. K., Wilson, W. David

Abstract

Biosensor-surface plasmon resonance (SPR) technology has emerged as a powerful label-free approach for the study of nucleic acid interactions in real time. The method provides simultaneous equilibrium and kinetic characterization for biomolecular interactions with low sample requirements and without the need for external probes. A detailed and practical guide for protein-DNA interaction analyses using biosensor-SPR methods is presented. Details of SPR technology and basic fundamentals are described with recommendations on the preparation of the SPR instrument, sensor chips and samples, experimental design, quantitative and qualitative data analyses and presentation. A specific example of the interaction of a transcription factor with DNA is provided with results evaluated by both kinetic and steady-state SPR methods.

Mendeley readers

Mendeley readers

The data shown below were compiled from readership statistics for 37 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Germany 1 3%
Unknown 36 97%

Demographic breakdown

Readers by professional status Count As %
Student > Bachelor 7 19%
Researcher 7 19%
Student > Ph. D. Student 6 16%
Student > Master 3 8%
Student > Doctoral Student 2 5%
Other 2 5%
Unknown 10 27%
Readers by discipline Count As %
Biochemistry, Genetics and Molecular Biology 15 41%
Agricultural and Biological Sciences 4 11%
Chemistry 2 5%
Pharmacology, Toxicology and Pharmaceutical Science 1 3%
Chemical Engineering 1 3%
Other 2 5%
Unknown 12 32%