TY - JOUR
T1 - The "correctly folded" state of proteins
T2 - Is it a metastable state?
AU - Gazit, Ehud
PY - 2002/1/18
Y1 - 2002/1/18
N2 - Alzheimer's disease, type H diabetes, Creutzfeldt-Jakob disease, and amyloid-related diseases: In each of these pathological situations, well-folded proteins undergo an irreversible transition from the "correctly folded" state to a collapsed β-sheet-rich structure. Here it is suggested that the aggregated form represents a global minimum in Gibbs energy for ensembles of protein molecules in general, and that at an infinite time any protein solution above a critical concentration will eventually undergo structural transition into the aggregated state.
AB - Alzheimer's disease, type H diabetes, Creutzfeldt-Jakob disease, and amyloid-related diseases: In each of these pathological situations, well-folded proteins undergo an irreversible transition from the "correctly folded" state to a collapsed β-sheet-rich structure. Here it is suggested that the aggregated form represents a global minimum in Gibbs energy for ensembles of protein molecules in general, and that at an infinite time any protein solution above a critical concentration will eventually undergo structural transition into the aggregated state.
KW - Aggregation
KW - Amyloidosis
KW - Protein folding
KW - Proteins
UR - http://www.scopus.com/inward/record.url?scp=0037126833&partnerID=8YFLogxK
U2 - 10.1002/1521-3773(20020118)41:2<257::AID-ANIE257>3.0.CO;2-M
DO - 10.1002/1521-3773(20020118)41:2<257::AID-ANIE257>3.0.CO;2-M
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AN - SCOPUS:0037126833
SN - 1433-7851
VL - 41
SP - 257
EP - 259
JO - Angewandte Chemie - International Edition
JF - Angewandte Chemie - International Edition
IS - 2
ER -
