Selection of carbonic anhydrase variants displayed on phage. Aromatic residues in zinc binding site enhance metal affinity and equilibration kinetics.
about
Probing the roles of two tryptophans surrounding the unique zinc coordination site in lipase family I.5Designing hydrolytic zinc metalloenzymesCarbonic anhydrase II-based metal ion sensing: Advances and new perspectives.Revisiting zinc coordination in human carbonic anhydrase II.Genetically encoded ratiometric biosensors to measure intracellular exchangeable zinc in Escherichia coli.Role of zinc in catalytic activity of carbonic anhydrase IX.The thermodynamics of protein interactions with essential first row transition metals.Carbonic anhydrase as a model for biophysical and physical-organic studies of proteins and protein-ligand binding.The wobble nucleotide-excising anticodon nuclease RloC is governed by the zinc-hook and DNA-dependent ATPase of its Rad50-like region.A de novo designed metalloenzyme for the hydration of CO2.Metal binding kinetics of bi-histidine sites used in psi analysis: evidence of high-energy protein folding intermediates.Thioredoxin 2, an oxidative stress-induced protein, contains a high affinity zinc binding site.Mobile trap algorithm for zinc detection using protein sensors.
P2860
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P2860
Selection of carbonic anhydrase variants displayed on phage. Aromatic residues in zinc binding site enhance metal affinity and equilibration kinetics.
description
1997 nî lūn-bûn
@nan
1997年の論文
@ja
1997年論文
@yue
1997年論文
@zh-hant
1997年論文
@zh-hk
1997年論文
@zh-mo
1997年論文
@zh-tw
1997年论文
@wuu
1997年论文
@zh
1997年论文
@zh-cn
name
Selection of carbonic anhydras ...... ty and equilibration kinetics.
@en
type
label
Selection of carbonic anhydras ...... ty and equilibration kinetics.
@en
prefLabel
Selection of carbonic anhydras ...... ty and equilibration kinetics.
@en
P2860
P356
P1476
Selection of carbonic anhydras ...... ty and equilibration kinetics.
@en
P2093
P2860
P304
20364-20372
P356
10.1074/JBC.272.33.20364
P407
P577
1997-08-01T00:00:00Z