Zulfiqar Ahmad - Department of Biological Sciences, East Tennessee State University

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Zulfiqar Ahmad - Department of Biological Sciences, East Tennessee State University

Role of Asn-243 in the Phosphate-binding Subdomain of Catalytic Sites of Escherichia coli F1-ATPase*
Inhibition of the ATPase activity of Escherichia coli ATP synthase by magnesium fluoride
ELSEVIER Biochimica et Biophysica Acta 1294 (1996) 63-71 Biochi~ic~aetBiophysicaA~ta
Involvement of ATP synthase residues aArg-376, bArg-182, and bLys-155 in Pi binding
Modulation of Charge in the Phosphate Binding Site of Escherichia coli ATP Synthase*
Role of -Subunit VISIT-DG Sequence Residues Ser-347 and Gly-351 in the Catalytic Sites of Escherichia coli ATP Synthase*
International Journal of Biological Macromolecules 45 (2009) 7279 Contents lists available at ScienceDirect
Abstract Similar neural network models based on single sequence and evolutionary profiles of residues have been
This article was published in an Elsevier journal. The attached copy is furnished to the author for non-commercial research and
Mutagenesis of Residue Arg-246 in the Phosphate-binding Subdomain of Catalytic Sites of Escherichia coli F1-ATPase*
Human Biliverdin Reductase Is a Leucine Zipper-like DNA-binding Protein and Functions in Transcriptional Activation of Heme
Role of Arg-166 in Yeast Cytochrome c1* Received for publication, January 19, 2001
Journal of Bioenergetics and Biomembranes, Vol. 37, No. 6, December 2005 ( C 2005) DOI: 10.1007/s10863-005-9486-8