NDLI: Structural heterogeneity of the various forms of apomyoglobin: implications for protein folding.

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: 1997 Volume: 6 Issue: 12

Year: 1997 Volume: 6 Issue: 11

Year: 1997 Volume: 6 Issue: 10

Sequence analysis of the AAA protein family.

Calcium binding to tandem repeats of EGF-like modules. Expression and characterization of the EGF-like modules of human Notch-1 implicated in receptor-ligand interactions.

Ideal architecture of residue packing and its observation in protein structures.

Unusual conformation of nicotinamide adenine dinucleotide (NAD) bound to diphtheria toxin: a comparison with NAD bound to the oxidoreductase enzymes.

The structures of thymidine kinase from herpes simplex virus type 1 in complex with substrates and a substrate analogue.

Phosphorylation on histidine is accompanied by localized structural changes in the phosphocarrier protein, HPr from Bacillus subtilis.

Identification and characterization of glycosylation sites in human serum clusterin.

Structural heterogeneity of the various forms of apomyoglobin: implications for protein folding.

Evaluating the energetics of empty cavities and internal mutations in proteins.

Dissection of the gene of the bifunctional PGK-TIM fusion protein from the hyperthermophilic bacterium Thermotoga maritima: design and characterization of the separate triosephosphate isomerase.

Ligand binding to proteins: the binding landscape model.

Glutathione S-transferase can be used as a C-terminal, enzymatically active dimerization module for a recombinant protease inhibitor, and functionally secreted into the periplasm of Escherichia coli.

Evidence for two conformational states of thioredoxin reductase from Escherichia coli: use of intrinsic and extrinsic quenchers of flavin fluorescence as probes to observe domain rotation.

DSC studies of the conformational stability of barstar wild-type.

Human recombinant [C22A] FK506-binding protein amide hydrogen exchange rates from mass spectrometry match and extend those from NMR.

Oligomerization properties of GCN4 leucine zipper e and g position mutants.

The specificity of carboxypeptidase Y may be altered by changing the hydrophobicity of the S'1 binding pocket.

Conformationally driven protease-catalyzed splicing of peptide segments: V8 protease-mediated synthesis of fragments derived from thermolysin and ribonuclease A.

Urea-induced conformational changes in cold- and heat-denatured states of a protein, Streptomyces subtilisin inhibitor.

1H, 13C, and 15N backbone assignment and secondary structure of the receptor-binding domain of vascular endothelial growth factor.

Protein-protein crystal-packing contacts.

Identification, expression, and crystallization of the protease-resistant conserved domain of synapsin I.

Cloning, expression, and crystallization of a hyperthermophilic protein that is homologous to the eukaryotic translation initiation factor, eIF5A.

Year: 1997 Volume: 6 Issue: 9

Year: 1997 Volume: 6 Issue: 8

Year: 1997 Volume: 6 Issue: 7

Year: 1997 Volume: 6 Issue: 6

Year: 1997 Volume: 6 Issue: 5

Year: 1997 Volume: 6 Issue: 4

Year: 1997 Volume: 6 Issue: 3

Year: 1997 Volume: 6 Issue: 2

Year: 1997 Volume: 6 Issue: 1

Year: 1996 Volume: 5

Year: 1995 Volume: 4

Year: 1994 Volume: 3

Year: 1993 Volume: 2

Year: 1992 Volume: 1

Structural heterogeneity of the various forms of apomyoglobin: implications for protein folding.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Gilmanshin, R. Dyer, R. B. Callender, R. H.
Description	Country affiliation: United States Author Affiliation: Gilmanshin R ( Department of Physics, City College of the City University of New York, New York 10031, USA.)
Abstract	Temperature-induced denaturation transitions of different structural forms of apomyoglobin were studied monitoring intrinsic tryptophan fluorescence. It was found that the tryptophans are effectively screened from solvent both in native and acid forms throughout most of the temperature range tested. Thus, the tryptophans' surrounding do not show a considerable change in structure where major protein conformational transitions have been found in apomyoglobin using other techniques. At high temperatures and under strong destabilizing conditions, the tryptophans' fluorescence parameters show sigmoidal thermal denaturation. These results, combined with previous studies, show that the structure of this protein is heterogeneous, including native-like (tightly packed) and molten globule-like substructures that exhibit conformation (denaturation) transitions under different conditions of pH and temperature (and denaturants). The results suggest that the folding of this protein proceeds via two 'nucleation' events whereby native-like contacts are formed. One of these events, which involves AGH 'core' formation, appears to occur very early in the folding process, even before significant hydrophobic collapse in the rest of the protein molecule. From the current studies and other results, a rather detailed picture of the folding of myoglobin is presented, on the level of specific structures and their thermodynamical properties as well as formation kinetics.
ISSN	09618368
e-ISSN	1469896X
Journal	Protein Science
Issue Number	10
Volume Number	6
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	1997-10-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Apoproteins Chemistry Myoglobin Protein Folding Cold Temperature Hot Temperature Hydrogen-ion Concentration Osmolar Concentration Protein Denaturation Sodium Chloride Administration & Dosage Spectrometry, Fluorescence Research Support, U.s. Gov't, Non-p.h.s. 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