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Studying protein-DNA interactions using atomic force microscopy.


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.

SUBMITTER: Beckwitt EC 

PROVIDER: S-EPMC5762137 | biostudies-literature | 2018 Jan

REPOSITORIES: biostudies-literature

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Studying protein-DNA interactions using atomic force microscopy.

Beckwitt Emily C EC   Kong Muwen M   Van Houten Bennett B  

Seminars in cell & developmental biology 20170630


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  ...[more]

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