Altering the mouth of a hydrophobic pocket. Structure and kinetics of human carbonic anhydrase II mutants at residue Val-121
about
A human transmembrane protein-tyrosine-phosphatase, PTP zeta, is expressed in brain and has an N-terminal receptor domain homologous to carbonic anhydrasesMolecular basis of human carbonic anhydrase II deficiencyThe active site architecture of Pisum sativum beta -carbonic anhydrase is a mirror image of that of alpha -carbonic anhydrasesStructural study of X-ray induced activation of carbonic anhydrase.Fluoroalkyl and Alkyl Chains Have Similar Hydrophobicities in Binding to the “Hydrophobic Wall” of Carbonic AnhydraseDependence of Effective Molarity on Linker Length for an Intramolecular Protein−Ligand SystemReplacements in a conserved leucine cluster in the hydrophobic heme pocket of cytochrome cMelanoma-associated retinopathy: a paraneoplastic autoimmune complicationModel-free extraction of spin label position distributions from pseudocontact shift data.Revisiting zinc coordination in human carbonic anhydrase II.Characterization of a folding intermediate of human carbonic anhydrase II: probing local mobility by electron paramagnetic resonance.Comparison of electron paramagnetic resonance methods to determine distances between spin labels on human carbonic anhydrase IIGenetically encoded ratiometric biosensors to measure intracellular exchangeable zinc in Escherichia coli.Structural features that govern enzymatic activity in carbonic anhydrase from a low-temperature adapted fish, Chionodraco hamatus.Thermodynamic parameters for the association of fluorinated benzenesulfonamides with bovine carbonic anhydrase II.Carbonic anhydrase as a model for biophysical and physical-organic studies of proteins and protein-ligand binding.The nucleotide-binding site of Aquifex aeolicus LpxC.Dependence of avidity on linker length for a bivalent ligand-bivalent receptor model system.Human carbonic anhydrase II-cyanate inhibitor complex: putting the debate to rest.Selective precipitation and purification of monovalent proteins using oligovalent ligands and ammonium sulfate.Using covalent dimers of human carbonic anhydrase II to model bivalency in immunoglobulins.Crystal structure of human carbonic anhydrase II at 1.95 A resolution in complex with 667-coumate, a novel anti-cancer agentNovel disulfide engineering in human carbonic anhydrase II using the PAIRWISE side-chain geometry database.A nonessential role for Arg 55 in cyclophilin18 for catalysis of proline isomerization during protein folding.MetalPDB in 2018: a database of metal sites in biological macromolecular structures.
P2860
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P2860
Altering the mouth of a hydrophobic pocket. Structure and kinetics of human carbonic anhydrase II mutants at residue Val-121
description
1991 nî lūn-bûn
@nan
1991 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
1991 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
1991年の論文
@ja
1991年論文
@yue
1991年論文
@zh-hant
1991年論文
@zh-hk
1991年論文
@zh-mo
1991年論文
@zh-tw
1991年论文
@wuu
name
Altering the mouth of a hydrop ...... II mutants at residue Val-121
@ast
Altering the mouth of a hydrop ...... II mutants at residue Val-121
@en
Altering the mouth of a hydrop ...... II mutants at residue Val-121
@nl
type
label
Altering the mouth of a hydrop ...... II mutants at residue Val-121
@ast
Altering the mouth of a hydrop ...... II mutants at residue Val-121
@en
Altering the mouth of a hydrop ...... II mutants at residue Val-121
@nl
prefLabel
Altering the mouth of a hydrop ...... II mutants at residue Val-121
@ast
Altering the mouth of a hydrop ...... II mutants at residue Val-121
@en
Altering the mouth of a hydrop ...... II mutants at residue Val-121
@nl
P2093
P1476
Altering the mouth of a hydrop ...... II mutants at residue Val-121
@en
P2093
Calderone TL
Christianson DW
P304
17320-17325
P407
P577
1991-09-01T00:00:00Z