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

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Item Type:	Article
Title:	Structural properties of UMP-kinase from Escherichia coli: Modulation of protein solubility by pH and UTP
Creators Name:	Serina, L., Bucurenci, N., Gilles, A.M., Surewicz, W.K., Fabian, H., Mantsch, H.H., Takahashi, M., Petrescu, I., 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
Volume:	35
Number:	22
Page Range:	7003-7011
Date:	1 January 1996
PubMed:	View item in PubMed

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