Oxford University Press, Nucleic Acids Research, 7(33), p. e68-e68, 2005
DOI: 10.1093/nar/gni073
Oxford University Press, Nucleic Acids Research, 8(33), p. 2767-2767, 2005
DOI: 10.1093/nar/gki577
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Bending of DNA is a feature essential to the function of many DNA-binding proteins. Bending angles can be estimated with a variety of techniques, but most directly from images obtained using scanning force microscopy (SFM). Direct measurement of the bending angle using a tangent method often produces angles that deviate significantly from values obtained using other techniques. Here, we describe the application of SFM in combination with simulations of DNA as a means to estimate protein-induced bending angles in a reliable and unbiased fashion. In this manner, we were able to obtain accurate estimates for the bending angles induced by nuclear factor I, octamer-binding transcription factor 1, the human XPC-Rad23B complex and integration host factor [correction]