dc.creator | Fernandez, Ariel | |
dc.creator | Berry, Stephen R. | |
dc.date.accessioned | 2019-06-28T19:26:31Z | |
dc.date.accessioned | 2022-10-15T12:50:33Z | |
dc.date.available | 2019-06-28T19:26:31Z | |
dc.date.available | 2022-10-15T12:50:33Z | |
dc.date.created | 2019-06-28T19:26:31Z | |
dc.date.issued | 2003-03-04 | |
dc.identifier | Fernandez, Ariel; Berry, Stephen R.; Proteins with H-bond packing defects are highly interactive with lipid bilayers: Implications for amyloidogenesis; National Academy of Sciences; Proceedings of the National Academy of Sciences of The United States of America; 100; 5; 4-3-2003; 2391-2396 | |
dc.identifier | 0027-8424 | |
dc.identifier | http://hdl.handle.net/11336/78919 | |
dc.identifier | Electronic | |
dc.identifier | CONICET Digital | |
dc.identifier | CONICET | |
dc.identifier.uri | https://repositorioslatinoamericanos.uchile.cl/handle/2250/4388056 | |
dc.description.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. | |
dc.language | eng | |
dc.publisher | National Academy of Sciences | |
dc.relation | info:eu-repo/semantics/altIdentifier/url/https://www.pnas.org/content/100/5/2391 | |
dc.relation | info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1073/pnas.0335642100 | |
dc.rights | https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ | |
dc.rights | info:eu-repo/semantics/restrictedAccess | |
dc.subject | AMYLOID | |
dc.title | Proteins with H-bond packing defects are highly interactive with lipid bilayers: Implications for amyloidogenesis | |
dc.type | info:eu-repo/semantics/article | |
dc.type | info:ar-repo/semantics/artículo | |
dc.type | info:eu-repo/semantics/publishedVersion | |