NDLI: Prevalence of Temperature-Dependent Heat Capacity Changes in Protein-DNA Interactions

Content Provider	PubMed Central
Author	Liu, Chin-chi Richard, Allison J. Datta, Kausiki Licata, Vince J.
Abstract	A large, negative ΔCp of DNA binding is a thermodynamic property of the majority of sequence-specific DNA-protein interactions, and a common, but not universal property of non-sequence-specific DNA binding. In a recent study of the binding of Taq polymerase to DNA, we showed that both the full-length polymerase and its “Klentaq” large fragment bind to primed-template DNA with significant negative heat capacities. Herein, we have extended this analysis by analyzing this data for temperature-variable heat capacity effects (ΔΔCp), and have similarly analyzed an additional 47 protein-DNA binding pairs from the scientific literature. Over half of the systems examined can be easily fit to a function that includes a ΔΔCp parameter. Of these, 90% display negative ΔΔCp values, with the result that the ΔCp of DNA binding will become more negative with rising temperature. The results of this collective analysis have potentially significant consequences for current quantitative theories relating ΔCp values to changes in accessible surface area, which rely on the assumption of temperature invariance of the ΔCp of binding. Solution structural data for Klentaq polymerase demonstrate that the observed heat capacity effects are not the result of a coupled folding event.
Related Links	http://dx.doi.org/10.1529/biophysj.107.117697
Starting Page	3258
File Format	PDF
ISSN	15420086
e-ISSN	15420086
Journal	Biophysical Journal
Issue Number	8
Volume Number	94
Language	English
Publisher	The Biophysical Society
Publisher Date	2008-04-15
Access Restriction	Open
Rights Holder	The Biophysical Society
Subject Keyword	Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Biophysics

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

Electrostatic contributions to heat capacity changes of DNA-ligand binding.

A Monte Carlo simulation study of protein-induced heat capacity changes and lipid-induced protein clustering.

Entropy and heat capacity of DNA melting from temperature dependence of single molecule stretching.

Heat Capacity Changes Associated with DNA Duplex Formation: Salt- and Sequence-Dependent Effects†

Thermo- and Mesostabilizing Protein Interactions Identified by Temperature-Dependent Statistical Potentials

Macromolecular Crowding Effects on Two Homologs of Ribosomal Protein S16: Protein-Dependent Structural Changes and Local Interactions

Heat capacity of protein folding.

Heat capacity changes and hydrophobic interactions in the binding of FK506 and rapamycin to the FK506 binding protein.

Thermodynamics of DNA: heat capacity changes on duplex unfolding

Prevalence of Temperature-Dependent Heat Capacity Changes in Protein-DNA Interactions

Similar Documents

Electrostatic contributions to heat capacity changes of DNA-ligand binding.

A Monte Carlo simulation study of protein-induced heat capacity changes and lipid-induced protein clustering.

Entropy and heat capacity of DNA melting from temperature dependence of single molecule stretching.

Heat Capacity Changes Associated with DNA Duplex Formation: Salt- and Sequence-Dependent Effects†

Thermo- and Mesostabilizing Protein Interactions Identified by Temperature-Dependent Statistical Potentials

Macromolecular Crowding Effects on Two Homologs of Ribosomal Protein S16: Protein-Dependent Structural Changes and Local Interactions

Heat capacity of protein folding.

Heat capacity changes and hydrophobic interactions in the binding of FK506 and rapamycin to the FK506 binding protein.

Thermodynamics of DNA: heat capacity changes on duplex unfolding

Prevalence of Temperature-Dependent Heat Capacity Changes in Protein-DNA Interactions