Linked Life Data

8073284

Source:http://linkedlifedata.com/resource/pubmed/id/8073284

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5177
pubmed:dateCreated
1994-9-28
pubmed:abstractText
A family of uniform periodic polypeptides has been prepared by bacterial expression of the corresponding artificial genes, with the objective of exploring the potential for control of supramolecular organization in genetically engineered protein-based polymeric materials. The repeating units of the polypeptides consist of oligomeric alanyl-glycine sequences interspersed with glutamic acid residues inserted at intervals of 8 to 14 amino acids. Crystallization of such materials from formic acid produces beta-sheet structures in the solid state, as shown by vibrational spectroscopy, nuclear magnetic resonance spectroscopy, and wide-angle x-ray diffraction. The diffraction results, together with observations from electron microscopy, are consistent with the formation of needle-shaped lamellar crystals whose thickness is controlled by the periodicity of the primary sequence. These results can be used to control solid-state structure in macromolecular materials.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0036-8075
pubmed:author
pubmed:issnType
Print
pubmed:day
2
pubmed:volume
265
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1427-32
pubmed:dateRevised
2007-3-19
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Chemical sequence control of beta-sheet assembly in macromolecular crystals of periodic polypeptides.
pubmed:affiliation
Department of Polymer Science and Engineering, University of Massachusetts, Amherst 01003.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S.