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Structural properties of UMP-kinase from Escherichia coli: Modulation of protein solubility by pH and UTP

Item Type:Article
Title:Structural properties of UMP-kinase from Escherichia coli: Modulation of protein solubility by pH and UTP
Creators Name:Serina, L. and Bucurenci, N. and Gilles, A.M. and Surewicz, W.K. and Fabian, H. and Mantsch, H.H. and Takahashi, M. and Petrescu, I. and Batelier, G. and Barzu, O.
Keywords:Allosteric Regulation, Base Sequence, Circular Dichroism, DNA Primers, Escherichia Coli, Fluorescence Spectrometry, Fourier Transform Infrared Spectroscopy, Hydrogen-Ion Concentration, Kinetics, Molecular Sequence Data, Nucleoside-Phosphate Kinase, Nucleotides, Protein Conformation, Protein Denaturation, Protein Folding, Secondary Protein Structure, Site-Directed Mutagenesis, Solubility, Tertiary Protein Structure, Ultracentrifugation, Uridine Triphosphate
Source:Biochemistry
ISSN:0006-2960
Publisher:American Chemical Society (U.S.A.)
Volume:35
Number:22
Page Range:7003-7011
Date:1 January 1996
PubMed:View item in PubMed

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