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Copper binding in the prion protein

Article Abstract:

A conformational change of the prion protein is responsible for the neurodegenerative diseases called the tranmissible spongiform encephalopathies, like mad cow disease and the human afflictions kuruand Creutzfeldt-Jakob disease. Prion protein is a copper binding protein with high selectivity for Cu(super 2+), which provides insight into the role of metals in neurodegenerative disease.

Author: Millhauser, Glenn L.
Publisher: American Chemical Society
Publication Name: Accounts of Chemical Research
Subject: Science and technology
ISSN: 0001-4842
Year: 2004
Causes of, Prion diseases

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Tyrosine-derived quinone cofactors

Article Abstract:

Both copper amine oxidases (CAOs) and lysyl oxidase (LOX) contain Cu(super 2+) and quinone cofactors, which are derived from a tyrosine residue in the active site. The properties of a model compound of lysine tyrosyl quinone (LTQ) and their relevance to the chemistry of LOX are discussed.

Author: Mure, Minae
Publisher: American Chemical Society
Publication Name: Accounts of Chemical Research
Subject: Science and technology
ISSN: 0001-4842
Year: 2004
Amino acids, Lysine

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Loops, linkages, rings, catenanes, cages, and crowders: entropy-based strategies for stabilizing proteins

Article Abstract:

A protein molecule exists in either a compact folded state or variable state, as preferred by chain entropy. An analysis of various entropy-based stabilization strategies with the help of polymer theory-based models is presented.

Author: Huan-Xiang Zhou
Publisher: American Chemical Society
Publication Name: Accounts of Chemical Research
Subject: Science and technology
ISSN: 0001-4842
Year: 2004
Entropy (Physics), Entropy (Thermodynamics), Chemical models

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Subjects list: Research, Analysis, Proteins, Chemical bonds, Copper compounds, Atomic properties
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