| Literature DB >> 28673677 |
Emily C Beckwitt1, Muwen Kong1, Bennett Van Houten2.
Abstract
Atomic force microscopy (AFM) has made significant contributions to the study of protein-DNA interactions by making it possible to topographically image biological samples. A single protein-DNA binding reaction imaged by AFM can reveal protein binding specificity and affinity, protein-induced DNA bending, and protein binding stoichiometry. Changes in DNA structure, complex conformation, and cooperativity, can also be analyzed. In this review we highlight some important examples in the literature and discuss the advantages and limitations of these measurements. We also discuss important advances in technology that will facilitate the progress of AFM in the future.Entities:
Keywords: Atomic force microscopy; Binding specificity; DNA bending; Protein-DNA interaction; Stoichiometry
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Year: 2017 PMID: 28673677 PMCID: PMC5762137 DOI: 10.1016/j.semcdb.2017.06.028
Source DB: PubMed Journal: Semin Cell Dev Biol ISSN: 1084-9521 Impact factor: 7.727