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dc.contributor.author
Fernandez, Ariel
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dc.contributor.author
Berry, Stephen R.
dc.date.available
2019-06-28T19:26:31Z
dc.date.issued
2003-03-04
dc.identifier.citation
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.issn
0027-8424
dc.identifier.uri
http://hdl.handle.net/11336/78919
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.format
application/pdf
dc.language.iso
eng
dc.publisher
National Academy of Sciences
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dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
Amyloid
dc.subject.classification
Biofísica
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dc.subject.classification
Ciencias Biológicas
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dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
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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
dc.date.updated
2019-06-12T14:21:26Z
dc.identifier.eissn
Electronic
dc.journal.volume
100
dc.journal.number
5
dc.journal.pagination
2391-2396
dc.journal.pais
Estados Unidos
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dc.journal.ciudad
Washington
dc.description.fil
Fil: Fernandez, Ariel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca; Argentina. University of Chicago; Estados Unidos
dc.description.fil
Fil: Berry, Stephen R.. University of Chicago; Estados Unidos
dc.journal.title
Proceedings of the National Academy of Sciences of The United States of America
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dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://www.pnas.org/content/100/5/2391
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1073/pnas.0335642100
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