Linked Life Data

17616387

Source:http://linkedlifedata.com/resource/pubmed/id/17616387

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2007-9-17
pubmed:abstractText
Nature has long used peptide- and protein-based manufacturing to create structures whose remarkable mechanical, transport, optical, and even magnetic properties are determined by a fine control of composition and architecture extending from the nanoscale to the macroscale. Although there is much to learn from the tools and strategies that have been evolutionary selected for building biomaterials, accessing compositions and architectures of engineering interest is crucial to the development of the next generation of hybrid functional materials. In recent years, portable amino acid sequences selected from combinatorial libraries and supporting the assembly, nucleation, and geometrical organization of solid phases have emerged as attractive tools for bionanofabrication. Here, we review how these polypeptides are selected and progress in the understanding of their interaction with inorganic and synthetic materials.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0958-1669
pubmed:author
pubmed:issnType
Print
pubmed:volume
18
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
312-7
pubmed:meshHeading
pubmed:year
2007
pubmed:articleTitle
Selection and analysis of solid-binding peptides.
pubmed:affiliation
Department of Chemical Engineering, University of Washington, Box 351750, Seattle, WA 98195-1750, USA. baneyx@u.washington.edu
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S., Review