Calorimetric study of myoglobin embedded in trehalose-water matrixes
It has been suggested that in ‘dry’ protein-trehalose-water systems, water-mediated hydrogen bond network, whose strength increases by drying, anchors the protein to its surroundings. To further characterize this effect, we performed a DSC study on low-water myoglobin-trehalose systems. The denatura...
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Veröffentlicht in: | Journal of thermal analysis and calorimetry 2009-03, Vol.95 (3), p.699-702 |
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creator | Bellavia, G. Cordone, L. Cupane, A. |
description | It has been suggested that in ‘dry’ protein-trehalose-water systems, water-mediated hydrogen bond network, whose strength increases by drying, anchors the protein to its surroundings. To further characterize this effect, we performed a DSC study on low-water myoglobin-trehalose systems. The denaturation temperature resulted to increase by decreasing hydration, and linearly correlated to the glass transition temperature of both the ternary protein-water-trehalose and the binary water-trehalose systems. Further measurements are being performed to investigate eventual differences among different saccharides. |
doi_str_mv | 10.1007/s10973-008-9490-4 |
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To further characterize this effect, we performed a DSC study on low-water myoglobin-trehalose systems. The denaturation temperature resulted to increase by decreasing hydration, and linearly correlated to the glass transition temperature of both the ternary protein-water-trehalose and the binary water-trehalose systems. Further measurements are being performed to investigate eventual differences among different saccharides.</description><identifier>ISSN: 1388-6150</identifier><identifier>EISSN: 1588-2926</identifier><identifier>EISSN: 1572-8943</identifier><identifier>DOI: 10.1007/s10973-008-9490-4</identifier><language>eng</language><publisher>Dordrecht: Springer Netherlands</publisher><subject>Analytical Chemistry ; Analytical, structural and metabolic biochemistry ; Biological and medical sciences ; Biological Materials ; Chemistry ; Chemistry and Materials Science ; Fundamental and applied biological sciences. 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To further characterize this effect, we performed a DSC study on low-water myoglobin-trehalose systems. The denaturation temperature resulted to increase by decreasing hydration, and linearly correlated to the glass transition temperature of both the ternary protein-water-trehalose and the binary water-trehalose systems. Further measurements are being performed to investigate eventual differences among different saccharides.</description><subject>Analytical Chemistry</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Biological and medical sciences</subject><subject>Biological Materials</subject><subject>Chemistry</subject><subject>Chemistry and Materials Science</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Hemoproteins</subject><subject>Inorganic Chemistry</subject><subject>Measurement Science and Instrumentation</subject><subject>Metalloproteins</subject><subject>Physical Chemistry</subject><subject>Polymer Sciences</subject><subject>Proteins</subject><issn>1388-6150</issn><issn>1588-2926</issn><issn>1572-8943</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><recordid>eNp9kEtPwzAQhC0EElXpD-CWC9wMfsWPIypPqRIXOFtOvClBSVzsRNB_j6tUHDntrPzNyDsIXVJyQwlRt4kSozgmRGMjDMHiBC1oqTVmhsnTrHnWkpbkHK1SaivCKJGm1GaB7teuC7HtYYxtXaRx8vsiNEW_D9suVO1QQF-B9-CLrMcIHxlPgL_dCLHoXXb9QLpAZ43rEqyOc4neHx_e1s948_r0sr7b4JoLM2JgrKyMAS8b5gUo6vL_CCiiKRhNhfHKe-dkRZk3qhFaeZJXykoutJaGL9H1nLuL4WuCNNq-TTV0nRsgTMlyLoVUQmeQzmAdQ0oRGrvLN7q4t5TYQ2V2rszmyuyhMiuy5-oY7lLtuia6oW7Tn5FRRqQQMnNs5lJ-GrYQ7WeY4pDv_if8F37je1A</recordid><startdate>20090301</startdate><enddate>20090301</enddate><creator>Bellavia, G.</creator><creator>Cordone, L.</creator><creator>Cupane, A.</creator><general>Springer Netherlands</general><general>Springer</general><scope>IQODW</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7SR</scope><scope>7U5</scope><scope>8BQ</scope><scope>8FD</scope><scope>JG9</scope><scope>L7M</scope></search><sort><creationdate>20090301</creationdate><title>Calorimetric study of myoglobin embedded in trehalose-water matrixes</title><author>Bellavia, G. ; Cordone, L. ; Cupane, A.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c349t-e225b99ed6f2d4e71a2920e7081e98149d7ddaa6b12d97f487d0aa61253488693</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2009</creationdate><topic>Analytical Chemistry</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Biological and medical sciences</topic><topic>Biological Materials</topic><topic>Chemistry</topic><topic>Chemistry and Materials Science</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Hemoproteins</topic><topic>Inorganic Chemistry</topic><topic>Measurement Science and Instrumentation</topic><topic>Metalloproteins</topic><topic>Physical Chemistry</topic><topic>Polymer Sciences</topic><topic>Proteins</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Bellavia, G.</creatorcontrib><creatorcontrib>Cordone, L.</creatorcontrib><creatorcontrib>Cupane, A.</creatorcontrib><collection>Pascal-Francis</collection><collection>CrossRef</collection><collection>Engineered Materials Abstracts</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>METADEX</collection><collection>Technology Research Database</collection><collection>Materials Research Database</collection><collection>Advanced Technologies Database with Aerospace</collection><jtitle>Journal of thermal analysis and calorimetry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Bellavia, G.</au><au>Cordone, L.</au><au>Cupane, A.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Calorimetric study of myoglobin embedded in trehalose-water matrixes</atitle><jtitle>Journal of thermal analysis and calorimetry</jtitle><stitle>J Therm Anal Calorim</stitle><date>2009-03-01</date><risdate>2009</risdate><volume>95</volume><issue>3</issue><spage>699</spage><epage>702</epage><pages>699-702</pages><issn>1388-6150</issn><eissn>1588-2926</eissn><eissn>1572-8943</eissn><abstract>It has been suggested that in ‘dry’ protein-trehalose-water systems, water-mediated hydrogen bond network, whose strength increases by drying, anchors the protein to its surroundings. To further characterize this effect, we performed a DSC study on low-water myoglobin-trehalose systems. The denaturation temperature resulted to increase by decreasing hydration, and linearly correlated to the glass transition temperature of both the ternary protein-water-trehalose and the binary water-trehalose systems. Further measurements are being performed to investigate eventual differences among different saccharides.</abstract><cop>Dordrecht</cop><pub>Springer Netherlands</pub><doi>10.1007/s10973-008-9490-4</doi><tpages>4</tpages></addata></record> |
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subjects | Analytical Chemistry Analytical, structural and metabolic biochemistry Biological and medical sciences Biological Materials Chemistry Chemistry and Materials Science Fundamental and applied biological sciences. Psychology Hemoproteins Inorganic Chemistry Measurement Science and Instrumentation Metalloproteins Physical Chemistry Polymer Sciences Proteins |
title | Calorimetric study of myoglobin embedded in trehalose-water matrixes |
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