DNA groove preference shift upon phosphorylation of a protamine-like cationic peptide

Author:

Chhetri Khadka B.12ORCID,Jang Yun Hee345ORCID,Lansac Yves45ORCID,Maiti Prabal K.1ORCID

Affiliation:

1. Center for Condensed Matter Theory, Department of Physics, Indian Institute of Science, Bangalore 560012, India

2. Department of Physics, Prithvinarayan Campus, Tribhuvan University, Pokhara, Nepal

3. Department of Energy Science and Engineering, DGIST, Daegu 42988, Korea

4. GREMAN, CNRS UMR 7347, Université de Tours, 37200 Tours, France

5. Laboratoire de Physique des Solides, CNRS UMR 8502, Université Paris Saclay, 91405 Orsay, France

Abstract

Entropic and Enthalpic contributions to Gibbs free energy of binding in four DNA-peptide complexes. It is observed that the binding of a protamine-like cationic peptide to DNA is enthalpy-driven for both major and minor grooves of DNA.

Funder

Department of Science and Technology, Ministry of Science and Technology, India

National Research Foundation of Korea

Publisher

Royal Society of Chemistry (RSC)

Subject

Physical and Theoretical Chemistry,General Physics and Astronomy

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