NDLI: Isoprenyl diphosphate synthases: protein sequence comparisons, a phylogenetic tree, and predictions of secondary structure.

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: 1994 Volume: 3

Year: 1994 Volume: 3 Issue: 12

Year: 1994 Volume: 3 Issue: 11

Year: 1994 Volume: 3 Issue: 10

Year: 1994 Volume: 3 Issue: 9

Year: 1994 Volume: 3 Issue: 8

Year: 1994 Volume: 3 Issue: 7

Year: 1994 Volume: 3 Issue: 6

Year: 1994 Volume: 3 Issue: 5

Year: 1994 Volume: 3 Issue: 4

A structural role for arginine in proteins: multiple hydrogen bonds to backbone carbonyl oxygens.

The importance of anchorage in determining a strained protein loop conformation.

Analysis of protein transmembrane helical regions by a neural network.

De novo protein design using pairwise potentials and a genetic algorithm.

A proposal for a coherent mammalian histone H1 nomenclature correlated with amino acid sequences.

Models of the serine protease domain of the human antithrombotic plasma factor activated protein C and its zymogen.

Isoprenyl diphosphate synthases: protein sequence comparisons, a phylogenetic tree, and predictions of secondary structure.

DNA binding and bending by the transcription factors GAL4(62*) and GAL4(149*).

Heparin binding domain peptides of antithrombin III: analysis by isothermal titration calorimetry and circular dichroism spectroscopy.

Distribution of distances between the tryptophan and the N-terminal residue of melittin in its complex with calmodulin, troponin C, and phospholipids.

Slow-folding kinetics of ribonuclease-A by volume change and circular dichroism: evidence for two independent reactions.

Protein folding dynamics: the diffusion-collision model and experimental data.

Thermodynamics of barnase unfolding.

Matrix-assisted laser desorption mass spectrometric peptide mapping of proteins separated by two-dimensional gel electrophoresis: determination of phosphorylation in synapsin I.

The three-dimensional profile method using residue preference as a continuous function of residue environment.

Interaction of phlorizin, a potent inhibitor of the Na+/D-glucose cotransporter, with the NADPH-binding site of mammalian catalases.

Similarity between pyridoxal/pyridoxamine phosphate-dependent enzymes involved in dideoxy and deoxyaminosugar biosynthesis and other pyridoxal phosphate enzymes.

A structural basis for the interaction of urea with lysozyme.

Charge reversal at the P3' position in protein C optimally enhances thrombin affinity and activation rate.

Year: 1994 Volume: 3 Issue: 3

Year: 1994 Volume: 3 Issue: 2

Year: 1994 Volume: 3 Issue: 1

Year: 1993 Volume: 2

Year: 1992 Volume: 1

Isoprenyl diphosphate synthases: protein sequence comparisons, a phylogenetic tree, and predictions of secondary structure.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Chen, A. Kroon, P. A. Poulter, C. D.
Description	Author Affiliation: Chen A ( Department of Chemistry, University of Utah, Salt Lake City 84112.)
Abstract	Isoprenyl diphosphate synthases are ubiquitous enzymes that catalyze the basic chain-elongation reaction in the isoprene biosynthetic pathway. Pairwise sequence comparisons were made for 6 farnesyl diphosphate synthases, 6 geranylgeranyl diphosphate synthases, and a hexaprenyl diphosphate synthase. Five regions with highly conserved residues, two of which contain aspartate-rich DDXX(XX)D motifs found in many prenyltransferases, were identified. A consensus secondary structure for the group, consisting mostly of alpha-helices, was predicted for the multiply aligned sequences from amino acid compositions, computer assignments of local structure, and hydropathy indices. Progressive sequence alignments suggest that the 13 isoprenyl diphosphate synthases evolved from a common ancestor into 3 distinct clusters. The most distant separation is between yeast hexaprenyl diphosphate synthetase and the other enzymes. Except for the chromoplastic geranylgeranyl diphosphate synthase from Capsicum annuum, the remaining farnesyl and geranylgeranyl diphosphate synthases segregate into prokaryotic/archaebacterial and eukaryotic families.
ISSN	09618368
e-ISSN	1469896X
Journal	Protein Science
Issue Number	4
Volume Number	3
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	1994-04-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Alkyl And Aryl Transferases Phylogeny Protein Structure, Secondary Transferases Chemistry Amino Acid Sequence Animals Bacteria Enzymology Binding Sites Conserved Sequence Dimethylallyltranstransferase Genetics Metabolism Farnesyltranstransferase Geranyltranstransferase Molecular Sequence Data Mutagenesis, Site-directed Neurospora Crassa Plants Protein Binding Saccharomyces Cerevisiae Sequence Alignment 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