Circular dichroism investigation of Escherichia coli adenylate kinase

The authors examined by circular dichroism (CD) spectroscopy in far- and near-ultraviolet three different molecular forms of Escherichia coli adenylate kinase: the wild type protein, the enzyme carboxymethylated at a single cysteine residue (Cys-77), and the thermosensitive adenylate kinase. The aut...

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Bibliographic Details
Published in:The Journal of biological chemistry 1987-01, Vol.26 (6), p.2502-2506
Main Authors: Monnot, M, Gilles, A-M, Saint Girons, I, Michelson, S, Barzu, O, Fermandjian, S
Format: Article
Language:English
Subjects:
adenylate kinase
C.D
Escherichia coli
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Summary:The authors examined by circular dichroism (CD) spectroscopy in far- and near-ultraviolet three different molecular forms of Escherichia coli adenylate kinase: the wild type protein, the enzyme carboxymethylated at a single cysteine residue (Cys-77), and the thermosensitive adenylate kinase. The authors also examined the CD spectra of isolated peptides resulting from chemical cleavage of adenylate kinase at Cys-77. The recovery of ordered structures, indicated by CD spectroscopy, paralleled the recovery of catalytic activity.
ISSN:0021-9258