Thermodynamic study of Cu2+ binding to the DAHK and GHK peptides by isothermal titration calorimetry (ITC) with the weaker competitor glycine (Q57816817)

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article published in 2011

Language	Label	Description	Also known as
English	Thermodynamic study of Cu2+ binding to the DAHK and GHK peptides by isothermal titration calorimetry (ITC) with the weaker competitor glycine	article published in 2011

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scholarly article

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Thermodynamic study of Cu2+ binding to the DAHK and GHK peptides by isothermal titration calorimetry (ITC) with the weaker competitor glycine (English)

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1 reference

ChEBI release 2020-05-28

object named as

Peter Faller

5

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Mathias Winterhalter

object named as

Mathias Winterhalter

4

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3

object named as

Wojciech Bal

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author name string

Ana Trapaidze

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Christelle Hureau

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publication date

4 September 2011

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Journal of Biological Inorganic Chemistry

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17

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1

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37-47

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https://scigraph.springernature.com/pub.10.1007/s00775-011-0824-5

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Copper transfer from Cu-Abeta to human serum albumin inhibits aggregation, radical production and reduces Abeta toxicity.

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Spectropotentiometric analysis of metal binding to structural zinc-binding sites: accounting quantitatively for pH and metal ion buffering effects.

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The interaction of copper(II) and glycyl-l-histidyl-l-lysine, a growth-modulating tripeptide from plasma

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Isothermal titration calorimetry measurements of Ni(II) and Cu(II) binding to His, GlyGlyHis, HisGlyHis, and bovine serum albumin: a critical evaluation

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Structure of the glycyl-L-histidyl-L-lysine-copper(II) complex in solution

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Short peptides are not reliable models of thermodynamic and kinetic properties of the N-terminal metal binding site in serum albumin

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10.1007/S00775-011-0824-5

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