Characterization of a molten globule state of bovine carbonic anhydrase III: loss of asymmetrical environment of the aromatic residues has a profound effect on both the near- and far-UV CD spectrum (Q61962347)

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scientific article published in February 1999

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English	Characterization of a molten globule state of bovine carbonic anhydrase III: loss of asymmetrical environment of the aromatic residues has a profound effect on both the near- and far-UV CD spectrum	scientific article published in February 1999

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scholarly article

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10082939%20AND%20SRC:MED&resulttype=core&format=json

12 November 2019

Characterization of a molten globule state of bovine carbonic anhydrase III: loss of asymmetrical environment of the aromatic residues has a profound effect on both the near- and far-UV CD spectrum (English)

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Europe PubMed Central

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10082939%20AND%20SRC:MED&resulttype=core&format=json

12 November 2019

3

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12 November 2019

author name string

K Borén

1

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12 November 2019

P Andersson

2

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12 November 2019

U Carlsson

4

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12 November 2019

publication date

1 February 1999

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12 November 2019

Biochimica et Biophysica Acta

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12 November 2019

1430

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12 November 2019

1

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12 November 2019

111-118

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12 November 2019

Mapping the folding intermediate of human carbonic anhydrase II. Probing substructure by chemical reactivity and spin and fluorescence labeling of engineered cysteine residues

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Detection and characterization using circular dichroism and fluorescence spectroscopy of a stable intermediate conformation formed in the denaturation of bovine carbonic anhydrase with guanidinium chloride

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Characterization of folding intermediates of human carbonic anhydrase II: probing substructure by chemical labeling of SH groups introduced by site-directed mutagenesis

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Refined structure of human carbonic anhydrase II at 2.0 A resolution

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

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Refined structure of bovine carbonic anhydrase III at 2.0 A resolution

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Origins and molecular evolution of the carbonic anhydrase isozymes

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Purification and some properties of carbonic anhydrase from bovine skeletal muscle

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Structures of folding intermediates

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Assignment of the contribution of the tryptophan residues to the circular dichroism spectrum of human carbonic anhydrase II.

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A comparative CD study of carbonic anhydrase isoenzymes with different number of tryptophans: impact on calculation of secondary structure content

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3 The preparation of guanidine hydrochloride

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Rapid ion-exchange chromatography for preparative separation of proteins IV. Application to bovine carbonic anhydrase III from skeletal muscle

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Contribution of individual tryptophan residues to the fluorescence spectrum of native and denatured forms of human carbonic anhydrase II

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Experimental errors and their effect on analyzing circular dichroism spectra of proteins

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Effects of multiple replacements at a single position on the folding and stability of dihydrofolate reductase from Escherichia coli

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Role of zinc (II) in the refolding of guanidine hydrochloride denatured bovine carbonic anhydrase

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Denaturation and reactivation of human carbonic anhydrases in guanidine hydrochloride and urea

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The carbonic anhydrases: widening perspectives on their evolution, expression and function

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Folding and stability of the N-terminus of human carbonic anhydrase II

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Identifiers

10.1016/S0167-4838(98)00283-0

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10082939%20AND%20SRC:MED&resulttype=core&format=json

12 November 2019

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10082939%20AND%20SRC:MED&resulttype=core&format=json

12 November 2019

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