The aromatic circular dichroism spectrum as a probe for conformational changes in the active site environment of hemocyanins-Reference-Cited by-同舟云学术

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The aromatic circular dichroism spectrum as a probe for conformational changes in the active site environment of hemocyanins

Published:1992-03 Issue:1 Volume:1120 Page:24-32
ISSN:0167-4838
Container-title:Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
language:en
Short-container-title:Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology

Author:

Beltramini Mariano,Bubacco Luigi,Salvato Benedetto,Casella Luigi,Gullotti Michele,Garofani Stefano

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics,Structural Biology

Reference47 articles.

1. Copper Proteins and Copper Enzymes;Preaux,1984

2. Structure determination of Panulirus interruptus haemocyanin at 3.2 Å resolution

3. Crystal structure of hexameric haemocyanin from Panulirus interruptus refined at 3.2 Å resolution

4. Electron addition to the active site of Cancer magister haemocyanins. An ESR study of Cu(II) centres after γ-radiolysis

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1. Entrapment and characterization of functional allosteric conformers of hemocyanin in sol–gel matrices;RSC Advances;2016

2. Principles and Applications of Selective Biophysical Methods for Characterization and Comparability Assessment of a Monoclonal Antibody;Current Pharmaceutical Biotechnology;2012-07-01

3. Raman, UV–vis, and CD Spectroscopic Studies of Dodecameric Oxyhemocyanin fromCarcinus aestuarii;Chemistry Letters;2011-12-05

4. Some kinetic properties of deoxytyrosinase;Journal of Molecular Catalysis B: Enzymatic;2010-02

5. The Ni(II)-Binding Properties of the Metallochaperone SlyD;Journal of the American Chemical Society;2009-11-30

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