Solution structure of thermostable cytochrome c-552 from Hydrogenobacter thermophilus determined by 1H-NMR spectroscopy
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Solution structure of the functional domain of Paracoccus denitrificans cytochrome c552 in the reduced stateSelected mutations in a mesophilic cytochrome c confer the stability of a thermophilic counterpartA Study of Ion-Neutral Collision Cross Section Values for Low Charge States of Peptides, Proteins, and Peptide/Protein Complexes.NMR and CD conformational studies of the C-terminal 16-peptides of Pseudomonas aeruginosa c551 and Hydrogenobacter thermophilus c552 cytochromes.In vitro formation of a c-type cytochrome.NMR and DFT investigation of heme ruffling: functional implications for cytochrome cHeme axial methionine fluxionality in Hydrogenobacter thermophilus cytochrome c552.Cytochrome c from a thermophilic bacterium has provided insights into the mechanisms of protein maturation, folding, and stability.The heme chaperone ApoCcmE forms a ternary complex with CcmI and apocytochrome cConversion of a c type cytochrome to a b type that spontaneously forms in vitro from apo protein and heme: implications for c type cytochrome biogenesis and folding.A cytochrome c from a lupanine-transforming Pseudomonas putida strain is expressed in Escherichia coli during aerobic cultivation and efficiently exported and assembled in the periplasm.Comparison of the backbone dynamics of wild-type Hydrogenobacter thermophilus cytochrome c(552) and its b-type variant.Variation and analysis of second-sphere interactions and axial histidinate character in c-type cytochromes.Cloning, expression, crystallization and preliminary X-ray characterization of cytochrome c552 from a moderate thermophilic bacterium, Hydrogenophilus thermoluteolus.Variation of the axial haem ligands and haem-binding motif as a probe of the Escherichia coli c-type cytochrome maturation (Ccm) system.Five amino acid residues responsible for the high stability of Hydrogenobacter thermophilus cytochrome c552: reciprocal mutation analysis.Stabilization mechanism of cytochrome c552 from a moderately thermophilic bacterium, Hydrogenophilus thermoluteolus.Stabilization of Pseudomonas aeruginosa cytochrome c(551) by systematic amino acid substitutions based on the structure of thermophilic Hydrogenobacter thermophilus cytochrome c(552).The cytochrome c fold can be attained from a compact apo state by occupancy of a nascent heme binding site.Stereoselective in vitro formation of c-type cytochrome variants from Hydrogenobacter thermophilus containing only a single thioether bond.NMR analysis shows that a b-type variant of Hydrogenobacter thermophilus cytochrome c552 retains its native structure.Amyloid fibril formation by a helical cytochrome.
P2860
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P2860
Solution structure of thermostable cytochrome c-552 from Hydrogenobacter thermophilus determined by 1H-NMR spectroscopy
description
1998 nî lūn-bûn
@nan
1998 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
name
Solution structure of thermost ...... ermined by 1H-NMR spectroscopy
@ast
Solution structure of thermost ...... ermined by 1H-NMR spectroscopy
@en
Solution structure of thermost ...... ermined by 1H-NMR spectroscopy
@nl
type
label
Solution structure of thermost ...... ermined by 1H-NMR spectroscopy
@ast
Solution structure of thermost ...... ermined by 1H-NMR spectroscopy
@en
Solution structure of thermost ...... ermined by 1H-NMR spectroscopy
@nl
prefLabel
Solution structure of thermost ...... ermined by 1H-NMR spectroscopy
@ast
Solution structure of thermost ...... ermined by 1H-NMR spectroscopy
@en
Solution structure of thermost ...... ermined by 1H-NMR spectroscopy
@nl
P2093
P356
P1433
P1476
Solution structure of thermost ...... ermined by 1H-NMR spectroscopy
@en
P2093
J Hasegawa
K Yamazaki
T Yamazaki
Y Igarashi
Y Kobayashi
Y Sambongi
P304
P356
10.1021/BI9803067
P407
P577
1998-07-07T00:00:00Z