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Conformation-dependent affinity of Cu(II) ions peptide complexes derived from the human Pin1 protein...

Conformation-dependent affinity of Cu(II) ions peptide complexes derived from the human Pin1 protein...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_crossref_primary_10_1007_s10973_016_5387_9

Conformation-dependent affinity of Cu(II) ions peptide complexes derived from the human Pin1 protein: ITC and DSC study

About this item

Full title

Conformation-dependent affinity of Cu(II) ions peptide complexes derived from the human Pin1 protein: ITC and DSC study

Publisher

Dordrecht: Springer Netherlands

Journal title

Journal of thermal analysis and calorimetry, 2017-02, Vol.127 (2), p.1431-1443

Language

English

Formats

Publication information

Publisher

Dordrecht: Springer Netherlands

More information

Scope and Contents

Contents

The human Pin1 WW domain catalyzes the
cis

trans
isomerization of the proline peptide bond. In this study, the conformation and binding of Cu(II) ions by Pin1 were investigated. It has been found that the affinity of peptide fragments of the human Pin1 WW domain for Cu(II) ions depends on its conformation. In particular, we analyzed t...

Alternative Titles

Full title

Conformation-dependent affinity of Cu(II) ions peptide complexes derived from the human Pin1 protein: ITC and DSC study

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_crossref_primary_10_1007_s10973_016_5387_9

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_crossref_primary_10_1007_s10973_016_5387_9

Other Identifiers

ISSN

1388-6150

E-ISSN

1588-2926

DOI

10.1007/s10973-016-5387-9

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