NDLI: Recognition of partially-folded mitochondrial malate dehydrogenase by GroEL. Steady and time-dependent emission anisotropy measurements.

Please wait, while we are loading the content...

Year: 2017 Volume: 26

Year: 2016 Volume: 25

Year: 2015 Volume: 24

Year: 2014 Volume: 23

Year: 2013 Volume: 22

Year: 2012 Volume: 21

Year: 2011 Volume: 20

Year: 2010 Volume: 19

Year: 2009 Volume: 18

Year: 2008 Volume: 17

Year: 2007 Volume: 16

Year: 2006 Volume: 15

Year: 2005 Volume: 14

Year: 2004 Volume: 13

Year: 2003 Volume: 12

Year: 2002 Volume: 11

Year: 2001 Volume: 10

Year: 2000 Volume: 9

Year: 1999 Volume: 8

Year: 1998 Volume: 7

Year: 1998 Volume: 7 Issue: 12

Structural analysis of inhibitor binding to human carbonic anhydrase II.

Solution structure of barley lipid transfer protein complexed with palmitate. Two different binding modes of palmitate in the homologous maize and barley nonspecific lipid transfer proteins.

A homology identification method that combines protein sequence and structure information.

Crystal structure of the effector-binding domain of the trehalose-repressor of Escherichia coli, a member of the LacI family, in its complexes with inducer trehalose-6-phosphate and noninducer trehalose.

Identification of kinetically hot residues in proteins.

Pulmonary surfactant-associated polypeptide C in a mixed organic solvent transforms from a monomeric alpha-helical state into insoluble beta-sheet aggregates.

The crystal structure of NADPH:ferredoxin reductase from Azotobacter vinelandii.

Dominant role of local dipolar interactions in phosphate binding to a receptor cleft with an electronegative charge surface: equilibrium, kinetic, and crystallographic studies.

Crystal structure of two quaternary complexes of dethiobiotin synthetase, enzyme-MgADP-AlF3-diaminopelargonic acid and enzyme-MgADP-dethiobiotin-phosphate; implications for catalysis.

Interaction of wheat alpha-thionin with large unilamellar vesicles.

Empirical solvent-mediated potentials hold for both intra-molecular and inter-molecular inter-residue interactions.

Recognition of partially-folded mitochondrial malate dehydrogenase by GroEL. Steady and time-dependent emission anisotropy measurements.

Domain structure analysis of elongation factor-3 from Saccharomyces cerevisiae by limited proteolysis and differential scanning calorimetry.

Localization of basic residues required for receptor binding to the single alpha-helix of the receptor binding domain of human alpha2-macroglobulin.

Self-organizing tree-growing network for the classification of protein sequences.

Probing the ligand binding domain of the GluR2 receptor by proteolysis and deletion mutagenesis defines domain boundaries and yields a crystallizable construct.

Unfolding and refolding of dimeric creatine kinase equilibrium and kinetic studies.

Effect of denaturant and protein concentrations upon protein refolding and aggregation: a simple lattice model.

Selective and asymmetric action of trypsin on the dimeric forms of seminal RNase.

Quantum chemical calculations of the reorganization energy of blue-copper proteins.

Solution structure of the His12 --> Cys mutant of the N-terminal zinc binding domain of HIV-1 integrase complexed to cadmium.

Ca2+-dependent conformational changes in bovine GCAP-2.

A solution SAXS study of Borrelia burgdorferi OspA, a protein containing a single-layer beta-sheet.

Yeast methionine aminopeptidase I can utilize either Zn2+ or Co2+ as a cofactor: a case of mistaken identity?

The trail to superoxide dismutase.

Year: 1998 Volume: 7 Issue: 11

Year: 1998 Volume: 7 Issue: 10

Year: 1998 Volume: 7 Issue: 9

Year: 1998 Volume: 7 Issue: 8

Year: 1998 Volume: 7 Issue: 7

Year: 1998 Volume: 7 Issue: 6

Year: 1998 Volume: 7 Issue: 5

Year: 1998 Volume: 7 Issue: 4

Year: 1998 Volume: 7 Issue: 3

Year: 1998 Volume: 7 Issue: 2

Year: 1998 Volume: 7 Issue: 1

Year: 1997 Volume: 6

Year: 1996 Volume: 5

Year: 1995 Volume: 4

Year: 1994 Volume: 3

Year: 1993 Volume: 2

Year: 1992 Volume: 1

Recognition of partially-folded mitochondrial malate dehydrogenase by GroEL. Steady and time-dependent emission anisotropy measurements.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Churchich, J. E.
Description	Country affiliation: United States Author Affiliation: Churchich JE ( Department of Biochemistry, University of Tennessee, Knoxville 37996-0840, USA. bcchurch@inet.polyn.edu.hk)
Abstract	The binding of partially-folded mitochondrial malate dehydrogenase (mMDH) to GroEL was assessed by steady and nanosecond emission spectroscopy. Partially-folded intermediates of mMDH show significant residual secondary structure when examined by CD spectroscopy in the far UV. They bind the extrinsic fluorescent probe ANS and the protein-ANS complexes display a rotational correlation time of 19 ns. Similar rotational correlation time (phi = 18.6 ns) was determined for partially-folded species tagged with anthraniloyl. GroEL recognizes partially-folded species with a K(D) approximately 60 nM. The rotational correlation time of the complex, i.e., GroEL-mMDH-ANT, approaches a value of 280 ns in the absence of ATP. Reactivation of mMDH-ANT by addition of GroEL and ATP brings about a significant decrease in the observed rotational correlation time. The results indicate that partially-folded malate dehydrogenase is rigidly trapped by GroEL in the absence of ATP, whereas addition of ATP facilitates reactivation and release of folded conformations endowed with catalytic activity.
ISSN	09618368
e-ISSN	1469896X
Journal	Protein Science
Issue Number	12
Volume Number	7
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	1998-12-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Anisotropy Chaperonin 60 Metabolism Malate Dehydrogenase Chemistry Mitochondria Enzymology Adenosine Triphosphate Phenylalanine Protein Denaturation Protein Folding Spectrometry, Fluorescence Time Factors Tyrosine Ortho-aminobenzoates Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

Central Library (ISO-9001:2015 Certified)
Indian Institute of Technology Kharagpur
Kharagpur, West Bengal, India | PIN - 721302

See location in the Map
03222 282435
Mail: support@ndl.gov.in

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