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Values of the kinetic constants derived from analyses of FRET traces shown in Fig. 8.
https://doi.org/10.1371/journal.pone.0078135.t002
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posted on 2013-10-30, 19:52
authored by
Toshifumi Mizuta
,
Kasumi Ando
,
Tatsuya Uemura
,
Yasushi Kawata
,
Tomohiro Mizobata
<p>Values of the kinetic constants derived from analyses of FRET traces shown in <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0078135#pone-0078135-g008" target="_blank">Fig. 8</a>.</p>
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Probing the Dynamic Process of Encapsulation in Escherichia coli GroEL
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Biophysics
Biochemistry
Microbiology
Cell Biology
Biotechnology
Chemical Sciences not elsewhere classified
Immunology
Biological Sciences not elsewhere classified
Developmental Biology
Plant Biology
Virology
Keywords
Dynamic Process
chaperonin function
GroEL apical domain
GroEL D 398A variants
apical domain movement
GroEL rings
GroEL SR
ATP binding
circularly permuted GroEL
polypeptide ends
GroES binding
Escherichia coli GroEL Kinetic analyses
CP
GroEL mutants
Helix M
ATP binding site
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CC BY 4.0
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