Antifreeze proteins: structures and mechanisms of function
Article Abstract:
The molecular structures of both the antifreeze glycoproteins (AFGP) and antifreeze proteins are rich in alanine. The peptide backbone in AFGP consists of alanine-alanine-threonine repeating tripeptide units and lack alpha-helix in their secondary structure. Antifreeze proteins function in a noncolligative antifreeze mechanism and the adsorption and desorption equilibrium of the antifreeze biomolecules is reversible. The activity of the antifreeze proteins is associated with nucleation inhibition and restriction of crystal growth. The structure of AFP proteins is discussed.
Publication Name: Chemical Reviews
Subject: Chemistry
ISSN: 0009-2665
Year: 1996
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Synthetic models for heme-copper oxidases
Article Abstract:
Synthetic models for heme-copper oxidases are discussed where heme-copper oxidases (HCOs) are the terminal respiratory enzymes to water without the release of superoxide or peroxide. Biomimetic model investigations are used to explore the fundamental aspects of structure, spectroscopy, magnetic and electronic structure, reactivity, and thus chemical mechanism.
Publication Name: Chemical Reviews
Subject: Chemistry
ISSN: 0009-2665
Year: 2004
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Electronic structures of metal sites in proteins and models: contributions to function in blue copper proteins
Article Abstract:
Different protein sites with the blue copper ligand set have different electronic structures. In case of the blue copper site, biomimetic studies have allowed perturbations of the nature of the thiolate and of the axial ligand and thus direct evaluation of these contributions to the spectroscopic features and electronic structure of the blue copper proteins.
Publication Name: Chemical Reviews
Subject: Chemistry
ISSN: 0009-2665
Year: 2004
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