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Enzymes for carbon sequestration: neutron crystallographic studies of carbonic anhydrase.

Enzymes for carbon sequestration: neutron crystallographic studies of carbonic anhydrase.

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Neutron diffraction studies towards deciphering the protonation state of catalytic residues in the bacterial KDN9P phosphatase.

P2860

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Enzymes for carbon sequestration: neutron crystallographic studies of carbonic anhydrase.

http://www.wikidata.org/entity/Q34257688

description

2010 nî lūn-bûn

@nan

2010 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի հոտեմբերին հրատարակված գիտական հոդված

@hy

2010年の論文

@ja

2010年論文

@yue

2010年論文

@zh-hant

2010年論文

@zh-hk

2010年論文

@zh-mo

2010年論文

@zh-tw

2010年论文

@wuu

name

Enzymes for carbon sequestration: neutron crystallographic studies of carbonic anhydrase.

@ast

Enzymes for carbon sequestration: neutron crystallographic studies of carbonic anhydrase.

@en

Enzymes for carbon sequestration: neutron crystallographic studies of carbonic anhydrase.

@nl

type

label

Enzymes for carbon sequestration: neutron crystallographic studies of carbonic anhydrase.

@ast

Enzymes for carbon sequestration: neutron crystallographic studies of carbonic anhydrase.

@en

Enzymes for carbon sequestration: neutron crystallographic studies of carbonic anhydrase.

@nl

prefLabel

Enzymes for carbon sequestration: neutron crystallographic studies of carbonic anhydrase.

@ast

Enzymes for carbon sequestration: neutron crystallographic studies of carbonic anhydrase.

@en

Enzymes for carbon sequestration: neutron crystallographic studies of carbonic anhydrase.

@nl

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Acta Crystallographica Section D: Biological Crystallography

P1476

Enzymes for carbon sequestration: neutron crystallographic studies of carbonic anhydrase.

@en

P2093

A Y Kovalevsky

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

D N Silverman

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

J Domsic

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

M Mustyakimov

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

P Langan

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

R McKenna

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

S Z Fisher

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

P2860

A short history of SHELX

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

Speeding up proton transfer in a fast enzyme: kinetic and crystallographic studies on the effect of hydrophobic amino acid substitutions in the active site of human carbonic anhydrase II

Entrapment of Carbon Dioxide in the Active Site of Carbonic Anhydrase II

Neutron Structure of Human Carbonic Anhydrase II: Implications for Proton Transfer

Structural and kinetic characterization of active-site histidine as a proton shuttle in catalysis by human carbonic anhydrase II

On the determinants of amide backbone exchange in proteins: a neutron crystallographic comparative study.

Preliminary joint neutron and X-ray crystallographic study of human carbonic anhydrase II.

Generalized X-ray and neutron crystallographic analysis: more accurate and complete structures for biological macromolecules

Elucidation of the proton transport mechanism in human carbonic anhydrase II.

P304

1178-1183

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

P31

scholarly article

P356

10.1107/S0907444910019700

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P433

Pt 11

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P478

66

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P577

2010-10-20T00:00:00Z

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P5875

47645185

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P698

21041933

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P921

carbon sequestration

P932

2967421

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