Linked Life Data

17550276

Source:http://linkedlifedata.com/resource/pubmed/id/17550276

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
14
pubmed:dateCreated
2007-6-26
pubmed:abstractText
The core recognition motif of the amyloidogenic beta-amyloid polypeptide, diphenylalanine peptide, has previously been shown to self-assemble into discrete, well-ordered, stiff nanotubes under mild conditions. The nanotubes keep the same morphology from room temperature up to 100 degrees C. In the presented study, we applied the bending beam model to atomic force microscopy images of diphenylalanine nanotubes suspended across cavities and obtained the Young's modulus 27 +/- 4 GPa and the shear modulus 0.21 +/- 0.03 GPa. We also showed that the elasticity of these nanotubes is stable within the same temperature range and at relative humidity from 0% to 70%. This study furthers our understanding of the structure and properties of these nanotubes, which are important for their potential applications in biotechnology.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0743-7463
pubmed:author
pubmed:issnType
Print
pubmed:day
3
pubmed:volume
23
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
7443-6
pubmed:meshHeading
pubmed:year
2007
pubmed:articleTitle
Using the bending beam model to estimate the elasticity of diphenylalanine nanotubes.
pubmed:affiliation
Laboratory of Biophysics and Surface Analysis, School of Pharmacy, The University of Nottingham, Nottingham NG7 2RD, U.K.
pubmed:publicationType
Journal Article