Biophysical characterization of DNA binding from single molecule force measurements.
作者： Kathy R. Chaurasiya , Thayaparan Paramanathan , Micah J. McCauley , Mark C. Williams
DOI: 10.1016/J.PLREV.2010.06.001
关键词:
摘要: Single molecule force spectroscopy is a powerful method that uses the mechanical properties of DNA to explore interactions. Here we describe how stretching experiments quantitatively characterize binding small molecules and proteins. Small exhibit diverse modes, including into major minor grooves intercalation between base pairs double-stranded (dsDNA). Histones bind package dsDNA, while other nuclear proteins such as high mobility group backbone bend dsDNA. Single-stranded (ssDNA) slide along dsDNA locate stabilize ssDNA during replication. Other both ssDNA. Nucleic acid chaperone can switch rapidly polymerases forms with affinity at distinct sites replication fork. measurements these mechanisms, elucidating interactions protein function.
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