NDLI: Probing the solution structure of the DNA-binding protein Max by a combination of proteolysis and mass spectrometry.

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: 1997 Volume: 6

Year: 1996 Volume: 5

Year: 1995 Volume: 4

Year: 1995 Volume: 4 Issue: 12

Year: 1995 Volume: 4 Issue: 11

Year: 1995 Volume: 4 Issue: 10

Year: 1995 Volume: 4 Issue: 9

Year: 1995 Volume: 4 Issue: 8

Year: 1995 Volume: 4 Issue: 7

Year: 1995 Volume: 4 Issue: 6

Covalent control of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase: insights into autoregulation of a bifunctional enzyme.

Quantitative measurements of the cooperativity in an EF-hand protein with sequential calcium binding.

Characterization of the N-terminal half-saturated state of calbindin D9k: NMR studies of the N56A mutant.

Identification of functionally important amino acids in the cellulose-binding domain of Trichoderma reesei cellobiohydrolase I.

A three-dimensional model of aromatase cytochrome P450.

Three-dimensional structure of the complex of 4-guanidino-Neu5Ac2en and influenza virus neuraminidase.

Probing the solution structure of the DNA-binding protein Max by a combination of proteolysis and mass spectrometry.

Quantitative approaches to utilizing mutational analysis and disulfide crosslinking for modeling a transmembrane domain.

A phage display system for studying the sequence determinants of protein folding.

Interaction of SecB with intermediates along the folding pathway of maltose-binding protein.

On the role of Glu-68 in alcohol dehydrogenase.

pH dependence of the stability of barstar to chemical and thermal denaturation.

Comparison of methods for searching protein sequence databases.

Incorporation of pairwise interactions into the Lifson-Roig model for helix prediction.

Domains in folding of model proteins.

Fuzzy cluster analysis of simple physicochemical properties of amino acids for recognizing secondary structure in proteins.

Automatic recognition of hydrophobic clusters and their correlation with protein folding units.

De novo prediction of polypeptide conformations using dihedral probability grid Monte Carlo methodology.

Building proteins from C alpha coordinates using the dihedral probability grid Monte Carlo method.

Crystallization and preliminary X-ray investigation of lipoxygenase-3 from soybeans.

Crystallization and preliminary X-ray crystallographic studies on Type III antifreeze protein.

Similarity of different beta-strands flanked in loops by glycines and prolines from distinct (alpha/beta)8-barrel enzymes: chance or a homology?

A putative FAD-binding domain in a distinct group of oxidases including a protein involved in plant development.

Year: 1995 Volume: 4 Issue: 5

Year: 1995 Volume: 4 Issue: 4

Year: 1995 Volume: 4 Issue: 3

Year: 1995 Volume: 4 Issue: 2

Year: 1995 Volume: 4 Issue: 1

Year: 1994 Volume: 3

Year: 1993 Volume: 2

Year: 1992 Volume: 1

Probing the solution structure of the DNA-binding protein Max by a combination of proteolysis and mass spectrometry.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Chait, B. T. Ferré-D'Amaré, A. R. Cohen, S. L. Burley, S. K.
Description	Country affiliation: United States Author Affiliation: Cohen SL ( Laboratory for Mass Spectrometry and Gaseous Ion Chemistry, Rockefeller University, New York, New York 10021, USA.)
Abstract	A simple biochemical method that combines enzymatic proteolysis and matrix-assisted laser desorption ionization mass spectrometry was developed to probe the solution structure of DNA-binding proteins. The method is based on inferring structural information from determinations of protection against enzymatic proteolysis, as governed by solvent accessibility and protein flexibility. This approach was applied to the study of the transcription factor Max--a member of the basic/helix-loop-helix/zipper family of DNA-binding proteins. In the absence of DNA and at low ionic strengths, Max is rapidly digested by each of six endoproteases selected for the study, results consistent with an open and flexible structure of the protein. At physiological salt levels, the rates of digestion are moderately slowed; this and the patterns of cleavage are consistent with homodimerization of the protein through a predominantly hydrophobic interface. In the presence of Max-specific DNA, the protein becomes dramatically protected against proteolysis, exhibiting up to a 100-fold reduction in cleavage rates. Over a 2-day period, both complete and partial proteolysis of the Max-DNA complex is observed. The partial proteolytic fragmentation patterns reflect a very high degree of protection in the N-terminal and helix-loop-helix regions of the protein, correlating with those expected of a stable dimer bound to DNA at its basic N-terminals. Less protection is seen at the C-terminal where a slow, sequential proteolytic cleavage occurs, correlating to the presence of a leucine zipper. The results also indicate a high affinity of Max for its target DNA that remains high even when the leucine zipper is proteolytically removed. In addition to the study of the helix-loop-helix protein Max, the present method appears well suited for a range of other structural biological applications.
ISSN	09618368
e-ISSN	1469896X
Journal	Protein Science
Issue Number	6
Volume Number	4
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	1995-06-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Dna-binding Proteins Chemistry Transcription Factors Amino Acid Sequence Basic Helix-loop-helix Leucine Zipper Transcription Factors Basic-leucine Zipper Transcription Factors Dna, Single-stranded Metabolism Helix-loop-helix Motifs Leucine Zippers Mass Spectrometry Models, Molecular Molecular Sequence Data Osmolar Concentration Peptide Mapping Protein Binding Serine Endopeptidases Subtilisins Comparative Study Research Support, Non-u.s. Gov't Research Support, U.s. Gov't, P.h.s. 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