Energetic rationale for an unexpected and abrupt reversal of guanidinium chloride-induced unfolding of peptide deformylase
about
Solvent-assisted slow conversion of a dithiazole derivative produces a competitive inhibitor of peptide deformylase.Delineation of alternative conformational states in Escherichia coli peptide deformylase via thermodynamic studies for the binding of actinonin.Peptide deformylase--a promising therapeutic target for tuberculosis and antibacterial drug discovery.
P2860
Energetic rationale for an unexpected and abrupt reversal of guanidinium chloride-induced unfolding of peptide deformylase
description
2007 nî lūn-bûn
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2007年の論文
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2007年論文
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2007年論文
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2007年論文
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2007年論文
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2007年論文
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2007年论文
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2007年论文
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2007年论文
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name
Energetic rationale for an une ...... folding of peptide deformylase
@en
Energetic rationale for an une ...... folding of peptide deformylase
@nl
type
label
Energetic rationale for an une ...... folding of peptide deformylase
@en
Energetic rationale for an une ...... folding of peptide deformylase
@nl
prefLabel
Energetic rationale for an une ...... folding of peptide deformylase
@en
Energetic rationale for an une ...... folding of peptide deformylase
@nl
P2093
P2860
P356
P1433
P1476
Energetic rationale for an une ...... folding of peptide deformylase
@en
P2093
Alexander K Berg
D K Srivastava
Daniel Eiler
Joel Kooren
P2860
P356
10.1110/PS.073270608
P577
2007-11-27T00:00:00Z