Conformational aspects of the Cu2+ binding to α-lactalbumin. Characterization and stability of the Cu-bound state
Author:
Publisher
Elsevier BV
Subject
Organic Chemistry,Biochemistry,Biophysics
Reference20 articles.
1. The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure
2. Interactions of Divalent Metal Ions with Bovine, Human, and Goat α-Lactalbumins1
3. Calcium binding effects on the structure of α-lactalbumin
4. Comparison of the binding of Na+ and Ca2+ to bovine α-lactalbumin
5. Hydrogen exchange of the tryptophan residues in bovine ?-lactalbumin studied by uv spectroscopy
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2. Disorder in Milk Proteins: α-Lactalbumin. Part C. Peculiarities of Metal Binding;Current Protein & Peptide Science;2016-10-04
3. One-pot peptide and protein conjugation: a combination of enzymatic transamidation and click chemistry;Chemical Communications;2016
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5. Speciation and isotope pattern deconvolution for inductively coupled plasma-mass spectrometry quantitative studies of mineral metabolism and supplementation;Pure and Applied Chemistry;2010-01-31
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