Abstract:
:We noticed that disease-related amyloidogenic proteins and especially cellular prion proteins have the highest proportion of incompletely desolvated backbone H bonds among soluble proteins. Such bonds are vulnerable to water attack and thus represent structural weaknesses. We have measured the adsorption of proteins onto phospholipid bilayers and found a strong correlation between the extent of underwrapping of backbone H bonds in the native structure of a protein and its extent of deposition on the bilayer: the less the H bond wrapping, the higher the propensity for protein-bilayer binding. These observations support the proposition that soluble proteins with amyloidogenic propensity and membrane proteins share a pervasive building motif: the underwrapped H bonds. Whereas in membrane proteins, this motif does not signal a structural vulnerability, in soluble proteins, it is responsible for their reactivity.
journal_name
Proc Natl Acad Sci U S Aauthors
Fernández A,Berry RSdoi
10.1073/pnas.0335642100keywords:
subject
Has Abstractpub_date
2003-03-04 00:00:00pages
2391-6issue
5eissn
0027-8424issn
1091-6490pii
0335642100journal_volume
100pub_type
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