Structure-assisted redesign of a protein-zinc-binding site with femtomolar affinity - Wikidata - wikimedia - TriplyDB

Structure-assisted redesign of a protein-zinc-binding site with femtomolar affinity

Structure-assisted redesign of a protein-zinc-binding site with femtomolar affinity

http://www.wikidata.org/entity/Q27730247

about

Protein design: toward functional metalloenzymes Crystal structure of E. coli β-carbonic anhydrase, an enzyme with an unusual pH-dependent activity Structure and metal binding properties of ZnuA, a periplasmic zinc transporter from Escherichia coli Designing hydrolytic zinc metalloenzymes Carbonic anhydrase II-based metal ion sensing: Advances and new perspectives.X-ray structure and mutational analysis of the atrazine Chlorohydrolase TrzN.The Loss and Gain of Functional Amino Acid Residues Is a Common Mechanism Causing Human Inherited Disease Carbonic anhydrase as a model for biophysical and physical-organic studies of proteins and protein-ligand binding.Metal-ion sites as structural and functional probes of helix-helix interactions in 7TM receptors.Mobile trap algorithm for zinc detection using protein sensors.

P2860

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P2860

Structure-assisted redesign of a protein-zinc-binding site with femtomolar affinity

http://www.wikidata.org/entity/Q27730247

description

1995 nî lūn-bûn

@nan

1995 թուականի Մայիսին հրատարակուած գիտական յօդուած

@hyw

1995 թվականի մայիսին հրատարակված գիտական հոդված

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1995年の論文

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1995年論文

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1995年論文

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1995年論文

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1995年論文

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1995年論文

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1995年论文

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name

Structure-assisted redesign of a protein-zinc-binding site with femtomolar affinity

@ast

Structure-assisted redesign of a protein-zinc-binding site with femtomolar affinity

@en

Structure-assisted redesign of a protein-zinc-binding site with femtomolar affinity

@nl

type

label

Structure-assisted redesign of a protein-zinc-binding site with femtomolar affinity

@ast

Structure-assisted redesign of a protein-zinc-binding site with femtomolar affinity

@en

Structure-assisted redesign of a protein-zinc-binding site with femtomolar affinity

@nl

prefLabel

Structure-assisted redesign of a protein-zinc-binding site with femtomolar affinity

@ast

Structure-assisted redesign of a protein-zinc-binding site with femtomolar affinity

@en

Structure-assisted redesign of a protein-zinc-binding site with femtomolar affinity

@nl

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PNAS.92.11.5017

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Proceedings of the National Academy of Sciences of the United States of America

P1476

Structure-assisted redesign of a protein-zinc-binding site with femtomolar affinity

@en

P2093

C A Fierke

http://www.w3.org/2001/XMLSchema#string

D W Christianson

http://www.w3.org/2001/XMLSchema#string

J A Ippolito

http://www.w3.org/2001/XMLSchema#string

S A McGee

http://www.w3.org/2001/XMLSchema#string

T T Baird

http://www.w3.org/2001/XMLSchema#string

P2860

Improved methods for building protein models in electron density maps and the location of errors in these models

Structure of native and apo carbonic anhydrase II and structure of some of its anion-ligand complexes

Engineering the hydrophobic pocket of carbonic anhydrase II

Structural and functional importance of a conserved hydrogen bond network in human carbonic anhydrase II

Structure of an engineered His3Cys zinc binding site in human carbonic anhydrase II

Engineering the zinc binding site of human carbonic anhydrase II: structure of the His-94-->Cys apoenzyme in a new crystalline form

Structure of an engineered, metal-actuated switch in trypsin

Crystallographic R factor refinement by molecular dynamics

Tertiary templates for proteins. Use of packing criteria in the enumeration of allowed sequences for different structural classes

The carbon dioxide hydration activity of carbonic anhydrase. I. Stop-flow kinetic studies on the native human isoenzymes B and C

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5017-21

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10.1073/PNAS.92.11.5017

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11

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92

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1995-05-23T00:00:00Z

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15438632

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7761440

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P921

protein structure

P932

41839

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