Carbonic Anhydrase: An Efficient Enzyme with Possible Global Implications
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Structural and biophysical characterization of the α-carbonic anhydrase from the gammaproteobacterium Thiomicrospira crunogena XCL-2: insights into engineering thermostable enzymes for CO2 sequestrationStructural and catalytic effects of proline substitution and surface loop deletion in the extended active site of human carbonic anhydrase IIMicrobial Carbonic Anhydrases in Biomimetic Carbon Sequestration for Mitigating Global Warming: Prospects and Perspectives.Dynamic encapsulation and activation of carbonic anhydrase in multivalent dynameric host matrices.Nickel Nanoparticles for Enhancing Carbon CaptureSolid-Binding Peptides: Immobilisation Strategies for Extremophile Biocatalysis in Biotechnology
P2860
Carbonic Anhydrase: An Efficient Enzyme with Possible Global Implications
description
article
@en
wetenschappelijk artikel
@nl
наукова стаття, опублікована у 2013
@uk
name
Carbonic Anhydrase: An Efficient Enzyme with Possible Global Implications
@en
Carbonic Anhydrase: An Efficient Enzyme with Possible Global Implications
@nl
type
label
Carbonic Anhydrase: An Efficient Enzyme with Possible Global Implications
@en
Carbonic Anhydrase: An Efficient Enzyme with Possible Global Implications
@nl
prefLabel
Carbonic Anhydrase: An Efficient Enzyme with Possible Global Implications
@en
Carbonic Anhydrase: An Efficient Enzyme with Possible Global Implications
@nl
P2093
P2860
P356
P1476
Carbonic Anhydrase: An Efficient Enzyme with Possible Global Implications
@en
P2093
Andrew Habibzadegan
Christopher D. Boone
Robert McKenna
Sonika Gill
P2860
P356
10.1155/2013/813931
P577
2013-01-01T00:00:00Z