Contributions of the Histidine Side Chain and the N-Terminal α-Amino Group to the Binding Thermodynamics of Oligopeptides to Nucleic Acids as a Function of pH-Reference-Cited by-同舟云学术

Contributions of the Histidine Side Chain and the N-Terminal α-Amino Group to the Binding Thermodynamics of Oligopeptides to Nucleic Acids as a Function of pH

Published:2010-02-11 Issue:9 Volume:49 Page:2018-2030
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Ballin Jeff D.¹,Prevas James P.¹,Ross Christina R.¹,Toth Eric A.¹,Wilson Gerald M.¹,Record M. Thomas²

Affiliation:

1. Department of Biochemistry and Molecular Biology and Marlene and Stewart Greenebaum Cancer Center, University of Maryland School of Medicine, Baltimore, Maryland 21201

2. Departments of Chemistry and Biochemistry, University of Wisconsin—Madison, Madison, Wisconsin 53706

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi902027z

Reference80 articles.

1. Structural Features of Protein−Nucleic Acid Recognition Sites

2. Classical Electrostatics in Biology and Chemistry

3. Structure-based analysis of protein-RNA interactions using the program ENTANGLE

4. Thermodynamic extent of counterion release upon binding oligolysines to single-stranded nucleic acids.

5. Thermodynamics of single-stranded RNA and DNA interactions with oligolysines containing tryptophan. Effects of base composition

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