Thermal stability of myosin rod from various species
The radius of gyration and fraction helix as a function of temperature have been determined for myosin rod from four different species: rabbit, frog, scallop, and antarctic fish. Measurements from sodium dodecyl sulfate gel electrophoresis indicate that all particles have the same molecular weight (...
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| Veröffentlicht in: | Biochemistry (Easton) 1987-12, Vol.26 (26), p.8703-8708 |
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| container_issue | 26 |
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| container_title | Biochemistry (Easton) |
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| creator | Rodgers, M. E Karr, T Biedermann, K Ueno, H Harrington, W. F |
| description | The radius of gyration and fraction helix as a function of temperature have been determined for myosin rod from four different species: rabbit, frog, scallop, and antarctic fish. Measurements from sodium dodecyl sulfate gel electrophoresis indicate that all particles have the same molecular weight (approximately 130K). All fragments are nearly 100% alpha-helical at low temperatures (0-5 degrees C). The melting profiles for each are qualitatively similar in shape, but their midpoints are shifted along the temperature axis in the following order: antarctic fish (Tm = 33 degrees C), scallop (Tm = 39 degrees C), frog (Tm = 45 degrees C), and rabbit (Tm = 49 degrees C). Corresponding radius of gyration vs temperature profiles for each species are shifted to lower temperatures (approximately 5-8 degrees C) with respect to the optical rotation melting curves. From plots of radius of gyration vs fraction helix, we find a marked drop in the radius of gyration (from 43 to approximately 34 nm) with less than a 5% decrease in fraction helix for rabbit, frog, and antarctic fish rods, whereas the radius of gyration of scallop rod never exceeds 34 nm. Results indicate hinging of the myosin rod of each species. The thermal stabilities of the myosin rods shift in parallel with the working temperature of their respective muscles. |
| doi_str_mv | 10.1021/bi00400a032 |
| format | Article |
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E ; Karr, T ; Biedermann, K ; Ueno, H ; Harrington, W. F</creator><creatorcontrib>Rodgers, M. E ; Karr, T ; Biedermann, K ; Ueno, H ; Harrington, W. F</creatorcontrib><description>The radius of gyration and fraction helix as a function of temperature have been determined for myosin rod from four different species: rabbit, frog, scallop, and antarctic fish. Measurements from sodium dodecyl sulfate gel electrophoresis indicate that all particles have the same molecular weight (approximately 130K). All fragments are nearly 100% alpha-helical at low temperatures (0-5 degrees C). The melting profiles for each are qualitatively similar in shape, but their midpoints are shifted along the temperature axis in the following order: antarctic fish (Tm = 33 degrees C), scallop (Tm = 39 degrees C), frog (Tm = 45 degrees C), and rabbit (Tm = 49 degrees C). Corresponding radius of gyration vs temperature profiles for each species are shifted to lower temperatures (approximately 5-8 degrees C) with respect to the optical rotation melting curves. From plots of radius of gyration vs fraction helix, we find a marked drop in the radius of gyration (from 43 to approximately 34 nm) with less than a 5% decrease in fraction helix for rabbit, frog, and antarctic fish rods, whereas the radius of gyration of scallop rod never exceeds 34 nm. Results indicate hinging of the myosin rod of each species. The thermal stabilities of the myosin rods shift in parallel with the working temperature of their respective muscles.</description><identifier>ISSN: 0006-2960</identifier><identifier>EISSN: 1520-4995</identifier><identifier>DOI: 10.1021/bi00400a032</identifier><identifier>PMID: 3502077</identifier><language>eng</language><publisher>Washington, DC: American Chemical Society</publisher><subject>Analytical, structural and metabolic biochemistry ; Animals ; Biological and medical sciences ; Contractile proteins ; Drug Stability ; Fishes ; Fundamental and applied biological sciences. Psychology ; Holoproteins ; Mollusca ; myosin ; Myosins - metabolism ; Optical Rotation ; Protein Conformation ; Protein Denaturation ; Proteins ; Rabbits ; Rana temporaria ; Species Specificity ; thermal stability ; Thermodynamics</subject><ispartof>Biochemistry (Easton), 1987-12, Vol.26 (26), p.8703-8708</ispartof><rights>1988 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a480t-f6093c3a78bee1927f38d4d7b0eb5ce493135ef5f8dd11b56a6483e8a4d5a90e3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/bi00400a032$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/bi00400a032$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>314,776,780,2752,27053,27901,27902,56713,56763</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=7822646$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/3502077$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Rodgers, M. E</creatorcontrib><creatorcontrib>Karr, T</creatorcontrib><creatorcontrib>Biedermann, K</creatorcontrib><creatorcontrib>Ueno, H</creatorcontrib><creatorcontrib>Harrington, W. F</creatorcontrib><title>Thermal stability of myosin rod from various species</title><title>Biochemistry (Easton)</title><addtitle>Biochemistry</addtitle><description>The radius of gyration and fraction helix as a function of temperature have been determined for myosin rod from four different species: rabbit, frog, scallop, and antarctic fish. Measurements from sodium dodecyl sulfate gel electrophoresis indicate that all particles have the same molecular weight (approximately 130K). All fragments are nearly 100% alpha-helical at low temperatures (0-5 degrees C). The melting profiles for each are qualitatively similar in shape, but their midpoints are shifted along the temperature axis in the following order: antarctic fish (Tm = 33 degrees C), scallop (Tm = 39 degrees C), frog (Tm = 45 degrees C), and rabbit (Tm = 49 degrees C). Corresponding radius of gyration vs temperature profiles for each species are shifted to lower temperatures (approximately 5-8 degrees C) with respect to the optical rotation melting curves. From plots of radius of gyration vs fraction helix, we find a marked drop in the radius of gyration (from 43 to approximately 34 nm) with less than a 5% decrease in fraction helix for rabbit, frog, and antarctic fish rods, whereas the radius of gyration of scallop rod never exceeds 34 nm. Results indicate hinging of the myosin rod of each species. The thermal stabilities of the myosin rods shift in parallel with the working temperature of their respective muscles.</description><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Contractile proteins</subject><subject>Drug Stability</subject><subject>Fishes</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Holoproteins</subject><subject>Mollusca</subject><subject>myosin</subject><subject>Myosins - metabolism</subject><subject>Optical Rotation</subject><subject>Protein Conformation</subject><subject>Protein Denaturation</subject><subject>Proteins</subject><subject>Rabbits</subject><subject>Rana temporaria</subject><subject>Species Specificity</subject><subject>thermal stability</subject><subject>Thermodynamics</subject><issn>0006-2960</issn><issn>1520-4995</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1987</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqF0E1rFEEQBuBGEuIac8o5MIeghzBaPf191KAxEIgmm4uXpmamGjvO7KzdsyH7751ll8WDkFMd3oei6mXslMMHDhX_WEcACYAgqldsxlUFpXROHbAZAOiychpeszc5P8LGGXnEjoSCCoyZMTn_RanHrsgj1rGL47oYQtGvhxwXRRraIqShL54wxWGVi7ykJlJ-yw4DdplOdvOYPXz9Mr_8Vt7cXl1ffropUVoYy6DBiUagsTURd5UJwrayNTVQrRqSTnChKKhg25bzWmnU0gqyKFuFDkgcs3fbvcs0_FlRHn0fc0NdhwuazvHGbj7S6kXIpVMwvTzBiy1s0pBzouCXKfaY1p6D35Tp_ylz0me7tau6p3Zvd-1N-fkux9xgFxIumpj3zNiq0lJPrNyymEd63seYfntthFF-_v3e6x_u7ie3nz2f_Putxyb7x2GVFlPJ_z3wL9mxldQ</recordid><startdate>19871201</startdate><enddate>19871201</enddate><creator>Rodgers, M. E</creator><creator>Karr, T</creator><creator>Biedermann, K</creator><creator>Ueno, H</creator><creator>Harrington, W. F</creator><general>American Chemical Society</general><scope>BSCLL</scope><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>C1K</scope><scope>7X8</scope></search><sort><creationdate>19871201</creationdate><title>Thermal stability of myosin rod from various species</title><author>Rodgers, M. E ; Karr, T ; Biedermann, K ; Ueno, H ; Harrington, W. F</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a480t-f6093c3a78bee1927f38d4d7b0eb5ce493135ef5f8dd11b56a6483e8a4d5a90e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1987</creationdate><topic>Analytical, structural and metabolic biochemistry</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Contractile proteins</topic><topic>Drug Stability</topic><topic>Fishes</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Holoproteins</topic><topic>Mollusca</topic><topic>myosin</topic><topic>Myosins - metabolism</topic><topic>Optical Rotation</topic><topic>Protein Conformation</topic><topic>Protein Denaturation</topic><topic>Proteins</topic><topic>Rabbits</topic><topic>Rana temporaria</topic><topic>Species Specificity</topic><topic>thermal stability</topic><topic>Thermodynamics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Rodgers, M. E</creatorcontrib><creatorcontrib>Karr, T</creatorcontrib><creatorcontrib>Biedermann, K</creatorcontrib><creatorcontrib>Ueno, H</creatorcontrib><creatorcontrib>Harrington, W. F</creatorcontrib><collection>Istex</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><jtitle>Biochemistry (Easton)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Rodgers, M. E</au><au>Karr, T</au><au>Biedermann, K</au><au>Ueno, H</au><au>Harrington, W. F</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Thermal stability of myosin rod from various species</atitle><jtitle>Biochemistry (Easton)</jtitle><addtitle>Biochemistry</addtitle><date>1987-12-01</date><risdate>1987</risdate><volume>26</volume><issue>26</issue><spage>8703</spage><epage>8708</epage><pages>8703-8708</pages><issn>0006-2960</issn><eissn>1520-4995</eissn><abstract>The radius of gyration and fraction helix as a function of temperature have been determined for myosin rod from four different species: rabbit, frog, scallop, and antarctic fish. Measurements from sodium dodecyl sulfate gel electrophoresis indicate that all particles have the same molecular weight (approximately 130K). All fragments are nearly 100% alpha-helical at low temperatures (0-5 degrees C). The melting profiles for each are qualitatively similar in shape, but their midpoints are shifted along the temperature axis in the following order: antarctic fish (Tm = 33 degrees C), scallop (Tm = 39 degrees C), frog (Tm = 45 degrees C), and rabbit (Tm = 49 degrees C). Corresponding radius of gyration vs temperature profiles for each species are shifted to lower temperatures (approximately 5-8 degrees C) with respect to the optical rotation melting curves. From plots of radius of gyration vs fraction helix, we find a marked drop in the radius of gyration (from 43 to approximately 34 nm) with less than a 5% decrease in fraction helix for rabbit, frog, and antarctic fish rods, whereas the radius of gyration of scallop rod never exceeds 34 nm. Results indicate hinging of the myosin rod of each species. The thermal stabilities of the myosin rods shift in parallel with the working temperature of their respective muscles.</abstract><cop>Washington, DC</cop><pub>American Chemical Society</pub><pmid>3502077</pmid><doi>10.1021/bi00400a032</doi><tpages>6</tpages></addata></record> |
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| source | MEDLINE; American Chemical Society Journals |
| subjects | Analytical, structural and metabolic biochemistry Animals Biological and medical sciences Contractile proteins Drug Stability Fishes Fundamental and applied biological sciences. Psychology Holoproteins Mollusca myosin Myosins - metabolism Optical Rotation Protein Conformation Protein Denaturation Proteins Rabbits Rana temporaria Species Specificity thermal stability Thermodynamics |
| title | Thermal stability of myosin rod from various species |
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