Chaperonin-mediated folding of green fluorescent protein.
about
Water Diffusion In And Out Of The β-Barrel Of GFP and The Fast Maturing Fluorescent Protein, TurboGFP.Biophysical characterization of natural and mutant fluorescent proteins cloned from zooxanthellate corals.Unfolding of Green Fluorescent Protein mut2 in wet nanoporous silica gels.Specific interaction between GroEL and denatured protein measured by compression-free force spectroscopy.Protein solubility and folding enhancement by interaction with RNAThe Protein Chaperone ClpX Targets Native and Non-native Aggregated Substrates for Remodeling, Disassembly, and Degradation with ClpPIdentification of sites for exponential translation in living dendrites.Troubleshooting coupled in vitro transcription-translation system derived from Escherichia coli cells: synthesis of high-yield fully active proteins.Acid-denatured Green Fluorescent Protein (GFP) as model substrate to study the chaperone activity of protein disulfide isomeraseConcerted ATP-induced allosteric transitions in GroEL facilitate release of protein substrate domains in an all-or-none manner.How do chaperonins fold protein?Effect of the C-terminal truncation on the functional cycle of chaperonin GroEL: implication that the C-terminal region facilitates the transition from the folding-arrested to the folding-competent state.A co-translational model to explain the in vivo import of proteins into HeLa cell mitochondriaThe Role of the Tight-Turn, Broken Hydrogen Bonding, Glu222 and Arg96 in the Post-translational Green Fluorescent Protein Chromophore Formation.Evidence for a specific microwave radiation effect on the green fluorescent protein.High salt-induced conversion of Escherichia coli GroEL into a fully functional thermophilic chaperonin.Trigger factor from Thermus thermophilus is a Zn2+-dependent chaperone.Discrimination of ATP, ADP, and AMPPNP by chaperonin GroEL: hexokinase treatment revealed the exclusive role of ATP.Successive and synergistic action of the Hsp70 and Hsp100 chaperones in protein disaggregation.Determination of the number of active GroES subunits in the fused heptamer GroES required for interactions with GroEL.Leu309 plays a critical role in the encapsulation of substrate protein into the internal cavity of GroEL.The interaction between electromagnetic fields at megahertz, gigahertz and terahertz frequencies with cells, tissues and organisms: risks and potential.On the maximum size of proteins to stay and fold in the cavity of GroEL underneath GroES.Local energetic frustration affects the dependence of green fluorescent protein folding on the chaperonin GroEL.Evaluation of the stability of an SR398/GroES chaperonin complex.Biomolecular robotics for chemomechanically driven guest delivery fuelled by intracellular ATP.Functional specialization in regulation and quality control in thermal adaptive evolution.Spectrally resolved microscopy of GFP trafficking.
P2860
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P2860
Chaperonin-mediated folding of green fluorescent protein.
description
1997 nî lūn-bûn
@nan
1997年の論文
@ja
1997年学术文章
@wuu
1997年学术文章
@zh-cn
1997年学术文章
@zh-hans
1997年学术文章
@zh-my
1997年学术文章
@zh-sg
1997年學術文章
@yue
1997年學術文章
@zh
1997年學術文章
@zh-hant
name
Chaperonin-mediated folding of green fluorescent protein.
@en
Chaperonin-mediated folding of green fluorescent protein.
@nl
type
label
Chaperonin-mediated folding of green fluorescent protein.
@en
Chaperonin-mediated folding of green fluorescent protein.
@nl
prefLabel
Chaperonin-mediated folding of green fluorescent protein.
@en
Chaperonin-mediated folding of green fluorescent protein.
@nl
P2093
P2860
P356
P1476
Chaperonin-mediated folding of green fluorescent protein.
@en
P2093
P2860
P304
12468-12474
P356
10.1074/JBC.272.19.12468
P407
P577
1997-05-01T00:00:00Z