What drives proteins into the major or minor grooves of DNA?

Abstract:

:The energetic profiles of a significant number of protein-DNA systems at 20 degrees C reveal that, despite comparable Gibbs free energies, association with the major groove is primarily an enthalpy-driven process, whereas binding to the minor groove is characterized by an unfavorable enthalpy that is compensated by favorable entropic contributions. These distinct energetic signatures for major versus minor groove binding are irrespective of the magnitude of DNA bending and/or the extent of binding-induced protein refolding. The primary determinants of their different energetic profiles appear to be the distinct hydration properties of the major and minor grooves; namely, that the water in the A+T-rich minor groove is in a highly ordered state and its removal results in a substantial positive contribution to the binding entropy. Since the entropic forces driving protein binding into the minor groove are a consequence of displacing water ordered by the regular arrangement of polar contacts, they cannot be regarded as hydrophobic.

journal_name

J Mol Biol

authors

Privalov PL,Dragan AI,Crane-Robinson C,Breslauer KJ,Remeta DP,Minetti CA

doi

10.1016/j.jmb.2006.09.059

subject

Has Abstract

pub_date

2007-01-05 00:00:00

pages

1-9

issue

1

eissn

0022-2836

issn

1089-8638

pii

S0022-2836(06)01284-8

journal_volume

365

pub_type

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