Atomic Force Microscopy of A-Gliadin Fibrils and in situ Degradation
Atomic force microscopy (AFM) has been used in air and in aqueous buffer to study the structure of fibrils formed by the self-assembly of A-gliadin protein molecules. The images showed fibrils with a diameter of between 15 and 30 nm and lengths ranging from about 100 nm to 2 μm. No branched fibrils...
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Veröffentlicht in: | Journal of cereal science 2000-05, Vol.31 (3), p.281-286 |
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container_title | Journal of cereal science |
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creator | McMaster, T.J. Miles, M.J. Kasarda, D.D. Shewry, P.R. Tatham, A.S. |
description | Atomic force microscopy (AFM) has been used in air and in aqueous buffer to study the structure of fibrils formed by the self-assembly of A-gliadin protein molecules. The images showed fibrils with a diameter of between 15 and 30 nm and lengths ranging from about 100 nm to 2 μm. No branched fibrils were observed, and there was no indication of a strong lateral inter-fibril interaction that would result in side-by-side association. Disassembly of the fibrils occurred when the pH of the aqueous buffer was reduced. In contrast the reverse process of fibril assembly and adsorption to the mica surface was less readily observed in situ. Some short fibrils were observed to assemble, but the lengths and densities were considerably less than those obtained by external deposition and drying. |
doi_str_mv | 10.1006/jcrs.2000.0307 |
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The images showed fibrils with a diameter of between 15 and 30 nm and lengths ranging from about 100 nm to 2 μm. No branched fibrils were observed, and there was no indication of a strong lateral inter-fibril interaction that would result in side-by-side association. Disassembly of the fibrils occurred when the pH of the aqueous buffer was reduced. In contrast the reverse process of fibril assembly and adsorption to the mica surface was less readily observed in situ. Some short fibrils were observed to assemble, but the lengths and densities were considerably less than those obtained by external deposition and drying.</description><subject>Animal, plant, fungal and microbial proteins, edible seaweeds and food yeasts</subject><subject>Biological and medical sciences</subject><subject>Food industries</subject><subject>Fundamental and applied biological sciences. 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Psychology</topic><topic>General aspects</topic><topic>gliadins, atomic force microscopy, scanning probe microscopy, A-gliadin fibrils, self-assembly</topic><topic>Methods of analysis, processing and quality control, regulation, standards</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>McMaster, T.J.</creatorcontrib><creatorcontrib>Miles, M.J.</creatorcontrib><creatorcontrib>Kasarda, D.D.</creatorcontrib><creatorcontrib>Shewry, P.R.</creatorcontrib><creatorcontrib>Tatham, A.S.</creatorcontrib><collection>Pascal-Francis</collection><collection>CrossRef</collection><jtitle>Journal of cereal science</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>McMaster, T.J.</au><au>Miles, M.J.</au><au>Kasarda, D.D.</au><au>Shewry, P.R.</au><au>Tatham, A.S.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Atomic Force Microscopy of A-Gliadin Fibrils and in situ Degradation</atitle><jtitle>Journal of cereal science</jtitle><date>2000-05-01</date><risdate>2000</risdate><volume>31</volume><issue>3</issue><spage>281</spage><epage>286</epage><pages>281-286</pages><issn>0733-5210</issn><eissn>1095-9963</eissn><coden>JCSCDA</coden><abstract>Atomic force microscopy (AFM) has been used in air and in aqueous buffer to study the structure of fibrils formed by the self-assembly of A-gliadin protein molecules. 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source | ScienceDirect Journals (5 years ago - present) |
subjects | Animal, plant, fungal and microbial proteins, edible seaweeds and food yeasts Biological and medical sciences Food industries Fundamental and applied biological sciences. Psychology General aspects gliadins, atomic force microscopy, scanning probe microscopy, A-gliadin fibrils, self-assembly Methods of analysis, processing and quality control, regulation, standards |
title | Atomic Force Microscopy of A-Gliadin Fibrils and in situ Degradation |
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