Thermal and Urea-Induced Unfolding of the Marginally Stable Lac Repressor DNA-Binding Domain: A Model System for Analysis of Solute Effects on Protein Processes-Reference-Cited by-同舟云学术

Thermal and Urea-Induced Unfolding of the Marginally Stable Lac Repressor DNA-Binding Domain: A Model System for Analysis of Solute Effects on Protein Processes

Published:2003-02-01 Issue:7 Volume:42 Page:2202-2217
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Felitsky Daniel J.¹,Record M. Thomas¹

Affiliation:

1. Department of Biochemistry and Department of Chemistry, University of Wisconsin-Madison, Madison, Wisconsin 53706

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi0270992

Reference73 articles.

1. Cooperative and Anticooperative Effects in Binding of the First and Second Plasmid OsymOperators to a LacI Tetramer: Evidence for Contributions of Non-operator DNA Binding by Wrapping and Looping

2. Wrapping of flanking non-operator DNA in lac repressor-operator complexes: implications for DNA looping 1 1Edited by R. Ebright

3. Repression oflacPromoter as a Function of Distance, Phase and Quality of an AuxiliarylacOperator

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