Source:http://linkedlifedata.com/resource/pubmed/id/12538909
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
11
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pubmed:dateCreated |
2003-1-22
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pubmed:abstractText |
Cysteine substitutions were engineered on the surface of maltose binding protein to produce crystine fibers, linear polymers of folded protein formed within a crystal. Disulfide bond formation between adjacent protein molecules within the lattice was monitored by X-ray crystallography. The cross-linked crystals were resistant to dissolution in water or neutral buffer solutions, even though the cross-linking was one-dimensional. However, crystine fibers were observed by transmission electron microscopy to dissociate from the crystals in acidic solutions. Some fibers remained associated as two-dimensional bundles or sheets, with a repeat unit along the fibers consistent with the packing of the individual protein molecules in the crystal. Neutralization of the acidic solutions caused the fibers to re-associate as a solid. Crystine threads were drawn out of this solution. In scanning electron microscopy images, many individual fibers could be seen unwinding from the ends of some threads. Crystine fibers are a new type of biomolecular material with potential applications wherever the use of proteins in a fibrous form is desirable, for example, the incorporation of enzymes into cloth or filtration material.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0269-2139
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
15
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
895-902
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:12538909-Carrier Proteins,
pubmed-meshheading:12538909-Crystallization,
pubmed-meshheading:12538909-Crystallography, X-Ray,
pubmed-meshheading:12538909-Maltose-Binding Proteins,
pubmed-meshheading:12538909-Microscopy, Electron,
pubmed-meshheading:12538909-Mutation,
pubmed-meshheading:12538909-Structure-Activity Relationship
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pubmed:year |
2002
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pubmed:articleTitle |
Crystine: fibrous biomolecular material from protein crystals cross-linked in a specific geometry.
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pubmed:affiliation |
Department of Chemistry, Rensselaer Polytechnic Institute, Troy, NY 12180, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.
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