NDLI: An optimized g-tensor for Rhodobacter capsulatus cytochrome c2 in solution: a structural comparison of the reduced and oxidized states.

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: 1996 Volume: 5 Issue: 12

Year: 1996 Volume: 5 Issue: 11

Year: 1996 Volume: 5 Issue: 10

Year: 1996 Volume: 5 Issue: 9

Covalent structure of the flavoprotein subunit of the flavocytochrome c: sulfide dehydrogenase from the purple phototrophic bacterium Chromatium vinosum.

Crystal structure of the 2[4Fe-4S] ferredoxin from Chromatium vinosum: evolutionary and mechanistic inferences for [3/4Fe-4S] ferredoxins.

Structural characterization of the tumor suppressor p16, an ankyrin-like repeat protein.

Peptide rescue of an N-terminal truncation of the Stoffel fragment of taq DNA polymerase.

Electrostatic effects in electron transfer reactions of [2Fe-2S] ferredoxins with inorganic reagents.

Improved genetic algorithm for the protein folding problem by use of a Cartesian combination operator.

An optimized g-tensor for Rhodobacter capsulatus cytochrome c2 in solution: a structural comparison of the reduced and oxidized states.

Denaturants can accelerate folding rates in a class of globular proteins.

Phage display of intact domains at high copy number: a system based on SOC, the small outer capsid protein of bacteriophage T4.

Circularly permuted dihydrofolate reductase possesses all the properties of the molten globule state, but can resume functional tertiary structure by interaction with its ligands.

Two partially unfolded states of Torpedo californica acetylcholinesterase.

Identification of protein kinase A phosphorylation sites on NBD1 and R domains of CFTR using electrospray mass spectrometry with selective phosphate ion monitoring.

High- and low-temperature unfolding of human high-density apolipoprotein A-2.

Binding sites for blood coagulation factor Xa and protein S involving residues 493-506 in factor Va.

Conformational stability of adrenodoxin mutant proteins.

A dynamic bundle of four adjacent hydrophobic segments in the denatured state of staphylococcal nuclease.

Coupling between trans/cis proline isomerization and protein stability in staphylococcal nuclease.

Dynamic NMR studies of ligand-receptor interactions: design and analysis of a rapidly exchanging complex of FKBP-12/FK506 with a 24 kDa calcineurin fragment.

Homology modeling of human methylmalonyl-CoA mutase: a structural basis for point mutations causing methylmalonic aciduria.

Purification and crystallization of cyclin-dependent kinase inhibitor p21.

Crystallization and preliminary X-ray diffraction studies of the Lb proteinase from foot-and-mouth disease virus.

Conformational flexibility and crystallization of tandemly linked type III modules of human fibronectin.

Members of the immunoglobulin superfamily in bacteria.

A fragment of staphylococcal nuclease with an OB-fold structure shows hydrogen-exchange protection factors in the range reported for 'molten globules'.

The chemical synthesis of proteins.

Year: 1996 Volume: 5 Issue: 8

Year: 1996 Volume: 5 Issue: 7

Year: 1996 Volume: 5 Issue: 6

Year: 1996 Volume: 5 Issue: 5

Year: 1996 Volume: 5 Issue: 4

Year: 1996 Volume: 5 Issue: 3

Year: 1996 Volume: 5 Issue: 2

Year: 1996 Volume: 5 Issue: 1

Year: 1995 Volume: 4

Year: 1994 Volume: 3

Year: 1993 Volume: 2

Year: 1992 Volume: 1

An optimized g-tensor for Rhodobacter capsulatus cytochrome c2 in solution: a structural comparison of the reduced and oxidized states.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Cusanovich, M. A. Zhao, D. Hutton, H. M. MacKenzie, N. E.
Description	Country affiliation: United States Author Affiliation: Zhao D ( Department of Pharmacology & Toxicology, College of Pharmacy, University of Arizona, Tucson 85721, USA. dzhao@ccit.arizona.edu)
Abstract	The optimized g-tensor parameters for the oxidized form of Rhodobacter capsulatus cytochrome c2 in solution were obtained using a set (50) of backbone amide protons. Dipolar shifts for more than 500 individual protons of R. capsulatus cytochrome c2 have been calculated by using the optimized g-tensor and the X-ray crystallographic coordinates of the reduced form of R. capsulatus cytochrome c2. The calculated results for dipolar shifts are compared with the observed paramagnetic shifts. The calculated and the observed data are in good agreement throughout the entire protein, but there are significant differences between calculated and experimental results localized to the regions in the immediate vicinity of the heme ligand and the region of the front crevice of the protein (residues 44-50, 53-57, and 61-68). The results not only indicate that the overall solution structures are very similar in both the reduced and oxidized states, but that these structures in solution are similar to the crystal structure. However, there are small structural changes near the heme and the rearrangement of certain residues that result in changes in their hydrogen bonding concomitant with the change in the oxidation states; this was also evident in the data for the NH exchange rate measurements for R. capsulatus cytochrome c2.
ISSN	09618368
e-ISSN	1469896X
Journal	Protein Science
Issue Number	9
Volume Number	5
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	1996-09-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Cytochrome c Group Chemistry Rhodobacter Capsulatus Chemical Phenomena Chemistry, Physical Crystallization Crystallography, X-ray Cytochromes C2 Heme Hydrogen Bonding Magnetic Resonance Spectroscopy Molecular Structure Oxidation-reduction Thermodynamics Comparative Study 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