NDLI: Differential Scanning Calorimetry of a Metalloprotein under Controlled Metal

Content Provider	Springer Nature Link
Author	Yasui, Masari Miyahara, Taku Aizawa, Tomoyasu Demura, Makoto Nitta, Katsutoshi
Copyright Year	2006
Abstract	In order to investigate the thermodynamics of the unfolding of metalloproteins, the thermal denaturation of bovine α-lactalbumin (BLA), a typical calcium-binding protein, was investigated under a wide variety of calcium ion activities by means of differential scanning calorimetry. The excess heat capacity obtained as above is composed of those of the following three reactions: (i) the release of a calcium ion from holo-BLA; (ii) the capture of the released calcium ion by the chelating reagent; and (iii) the denaturation of native apo-BLA. The results indicated that the presence of the chelating reagent had a remarkable effect on the apparent enthalpy change for the denaturation of holo-BLA. On the other hand, the influence of the chelator on the heat capacity change was shown to be negligible. Because the denaturation reaction of holo-BLA includes Reactions (i) and (iii), it had to be handled as a three-state reaction. Such an investigation of the unfolding has been scarcely found that the activity of the metal ion is controlled precisely in wide range.
Starting Page	475
Ending Page	482
Page Count	8
File Format	PDF
ISSN	15723887
Journal	The Protein Journal
Volume Number	25
Issue Number	7-8
e-ISSN	15734943
Language	English
Publisher	Kluwer Academic Publishers-Plenum Publishers
Publisher Date	2006-11-28
Publisher Place	New York
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Differential scanning calorimetry metalloprotein α-lactalbumin three-state unfolding enthalpy change of unfolding heat capacity change of unfolding Animal Anatomy / Morphology / Histology Organic Chemistry Biochemistry Bioorganic Chemistry
Content Type	Text
Resource Type	Article
Subject	Organic Chemistry Analytical Chemistry Biochemistry Bioengineering

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

An Irreversible and Kinetically Controlled Process: Thermal Induced Denaturation of L-2-Hydroxyisocaproate Dehydrogenase from Lactobacillus confusus

Denaturation Versus Unfolding: Energetic Aspects of Residual Structure in Denatured α-Lactalbumin

Influence of pH on the Structure and Oleic Acid Binding Ability of Bovine α-Lactalbumin

A Statistical Mechanical Deconvolution of the Differential Scanning Calorimetric Profiles of the Thermal Denaturation of Cyanomethemoglobin

Conformation-Dependent Interaction of α-Lactalbumin with Model and Biological Membranes: A Spin-Label ESR Study

Conformational Isomers of Denatured and Unfolded Proteins: Methods of Production and Applications

Osmolytic Effect of Sucrose on Thermal Denaturation of Pea Seedling Copper Amine Oxidase

The Effects of Molecular Crowding on the Amyloid Fibril Formation of α-Lactalbumin and the Chaperone Action of α-Casein

Two-State Folding of Lysozyme Versus Multiple-State Folding of α-Lactalbumin Illustrated by the Technique of Disulfide Scrambling

Differential Scanning Calorimetry of a Metalloprotein under Controlled Metal–Ion Activity

Similar Documents

An Irreversible and Kinetically Controlled Process: Thermal Induced Denaturation of L-2-Hydroxyisocaproate Dehydrogenase from Lactobacillus confusus

Denaturation Versus Unfolding: Energetic Aspects of Residual Structure in Denatured α-Lactalbumin

Influence of pH on the Structure and Oleic Acid Binding Ability of Bovine α-Lactalbumin

A Statistical Mechanical Deconvolution of the Differential Scanning Calorimetric Profiles of the Thermal Denaturation of Cyanomethemoglobin

Conformation-Dependent Interaction of α-Lactalbumin with Model and Biological Membranes: A Spin-Label ESR Study

Conformational Isomers of Denatured and Unfolded Proteins: Methods of Production and Applications

Osmolytic Effect of Sucrose on Thermal Denaturation of Pea Seedling Copper Amine Oxidase

The Effects of Molecular Crowding on the Amyloid Fibril Formation of α-Lactalbumin and the Chaperone Action of α-Casein

Two-State Folding of Lysozyme Versus Multiple-State Folding of α-Lactalbumin Illustrated by the Technique of Disulfide Scrambling

Differential Scanning Calorimetry of a Metalloprotein under Controlled Metal–Ion Activity