Temperature- and length-dependent energetics of formation for polyalanine helices in water: assignment of w(Ala)(n,T) and temperature-dependent CD ellipticity standards
Length-dependent helical propensities w(Ala)(n,T) at T = 10, 25, and 60 degrees C are assigned from t/c values and NMR 13C chemical shifts for series 1 peptides TrpLys(m)Inp2(t)Leu-Ala(n)(t)LeuInp2Lys(m)NH2, n = 15, 19, and 25, m = 5, in water. Van't Hoff analysis of w(Ala)(n,T) show that alpha...
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| Veröffentlicht in: | Journal of the American Chemical Society 2006-06, Vol.128 (25), p.8227-8233 |
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| creator | Job, Gabriel E Kennedy, Robert J Heitmann, Björn Miller, Justin S Walker, Sharon M Kemp, Daniel S |
| description | Length-dependent helical propensities w(Ala)(n,T) at T = 10, 25, and 60 degrees C are assigned from t/c values and NMR 13C chemical shifts for series 1 peptides TrpLys(m)Inp2(t)Leu-Ala(n)(t)LeuInp2Lys(m)NH2, n = 15, 19, and 25, m = 5, in water. Van't Hoff analysis of w(Ala)(n,T) show that alpha-helix formation is primarily enthalpy-driven. For series 2 peptides Ac-Trp Lys5Inp2(t)Leu-(beta)AspHel-Ala(n)-beta-(t)LeuInp2Lys5NH2, n = 12 and 22, which contain exceptionally helical Ala(n) cores, protection factor-derived fractional helicities FH are assigned in the range 10-30 degrees C in water and used to calibrate temperature-dependent CD ellipticities [theta](lambda,H,n,T). These are applied to CD data for series 1 peptides, 12 < or = n < or = 45, to confirm the w(Ala)(n,T) assignments at T = 25 and 60 degrees C. The [theta](lambda,H,n,T) are temperature dependent within the wavelength region, 222 +/- 12 nm, and yield a temperature correction for calculation of FH from experimental values of [theta](222,n,T,Exp). |
| doi_str_mv | 10.1021/ja060094y |
| format | Article |
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Van't Hoff analysis of w(Ala)(n,T) show that alpha-helix formation is primarily enthalpy-driven. For series 2 peptides Ac-Trp Lys5Inp2(t)Leu-(beta)AspHel-Ala(n)-beta-(t)LeuInp2Lys5NH2, n = 12 and 22, which contain exceptionally helical Ala(n) cores, protection factor-derived fractional helicities FH are assigned in the range 10-30 degrees C in water and used to calibrate temperature-dependent CD ellipticities [theta](lambda,H,n,T). These are applied to CD data for series 1 peptides, 12 < or = n < or = 45, to confirm the w(Ala)(n,T) assignments at T = 25 and 60 degrees C. The [theta](lambda,H,n,T) are temperature dependent within the wavelength region, 222 +/- 12 nm, and yield a temperature correction for calculation of FH from experimental values of [theta](222,n,T,Exp).</description><identifier>ISSN: 0002-7863</identifier><identifier>DOI: 10.1021/ja060094y</identifier><identifier>PMID: 16787087</identifier><language>eng</language><publisher>United States</publisher><subject>Circular Dichroism ; Computer Simulation ; Magnetic Resonance Spectroscopy ; Models, Chemical ; Molecular Structure ; Peptides - chemical synthesis ; Peptides - chemistry ; Protein Structure, Secondary ; Temperature ; Thermodynamics ; Water - chemistry</subject><ispartof>Journal of the American Chemical Society, 2006-06, Vol.128 (25), p.8227-8233</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16787087$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Job, Gabriel E</creatorcontrib><creatorcontrib>Kennedy, Robert J</creatorcontrib><creatorcontrib>Heitmann, Björn</creatorcontrib><creatorcontrib>Miller, Justin S</creatorcontrib><creatorcontrib>Walker, Sharon M</creatorcontrib><creatorcontrib>Kemp, Daniel S</creatorcontrib><title>Temperature- and length-dependent energetics of formation for polyalanine helices in water: assignment of w(Ala)(n,T) and temperature-dependent CD ellipticity standards</title><title>Journal of the American Chemical Society</title><addtitle>J Am Chem Soc</addtitle><description>Length-dependent helical propensities w(Ala)(n,T) at T = 10, 25, and 60 degrees C are assigned from t/c values and NMR 13C chemical shifts for series 1 peptides TrpLys(m)Inp2(t)Leu-Ala(n)(t)LeuInp2Lys(m)NH2, n = 15, 19, and 25, m = 5, in water. Van't Hoff analysis of w(Ala)(n,T) show that alpha-helix formation is primarily enthalpy-driven. For series 2 peptides Ac-Trp Lys5Inp2(t)Leu-(beta)AspHel-Ala(n)-beta-(t)LeuInp2Lys5NH2, n = 12 and 22, which contain exceptionally helical Ala(n) cores, protection factor-derived fractional helicities FH are assigned in the range 10-30 degrees C in water and used to calibrate temperature-dependent CD ellipticities [theta](lambda,H,n,T). These are applied to CD data for series 1 peptides, 12 < or = n < or = 45, to confirm the w(Ala)(n,T) assignments at T = 25 and 60 degrees C. The [theta](lambda,H,n,T) are temperature dependent within the wavelength region, 222 +/- 12 nm, and yield a temperature correction for calculation of FH from experimental values of [theta](222,n,T,Exp).</description><subject>Circular Dichroism</subject><subject>Computer Simulation</subject><subject>Magnetic Resonance Spectroscopy</subject><subject>Models, Chemical</subject><subject>Molecular Structure</subject><subject>Peptides - chemical synthesis</subject><subject>Peptides - chemistry</subject><subject>Protein Structure, Secondary</subject><subject>Temperature</subject><subject>Thermodynamics</subject><subject>Water - chemistry</subject><issn>0002-7863</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpNkM1OwzAQhH0A0VI48ALIJ9RKBOzETRxuVfmVKnEp52prb1pXiRNsR1XeiMck5Udwml1pdr7REnLB2Q1nMb_dAUsZy0V3RIaMsTjKZJoMyKn3u34VseQnZMDTTGZMZkPyscSqQQehdRhRsJqWaDdhG2ls0Gq0gaJFt8FglKd1QYvaVRBMbQ8TbeqygxKssUi3WBqFnhpL9xDQ3VHw3mxsdQjpL_fjWQmTsb1eTr5A4R_5jza_p1iWpul5JnTUh94KTvszclxA6fH8R0fk7fFhOX-OFq9PL_PZImp4kodIp0rxKYBQIkHRC8YcZSZlOtV5tk5AaAGFRqW1QK6KQkyBaZVrLrHQep2MyNV3buPq9xZ9WFXGq74SWKxbv0oly6WIs954-WNs1xXqVeNMBa5b_f42-QTuIH5H</recordid><startdate>20060628</startdate><enddate>20060628</enddate><creator>Job, Gabriel E</creator><creator>Kennedy, Robert J</creator><creator>Heitmann, Björn</creator><creator>Miller, Justin S</creator><creator>Walker, Sharon M</creator><creator>Kemp, Daniel S</creator><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope></search><sort><creationdate>20060628</creationdate><title>Temperature- and length-dependent energetics of formation for polyalanine helices in water: assignment of w(Ala)(n,T) and temperature-dependent CD ellipticity standards</title><author>Job, Gabriel E ; Kennedy, Robert J ; Heitmann, Björn ; Miller, Justin S ; Walker, Sharon M ; Kemp, Daniel S</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-p139t-d6cc15aa4c43e4a4ce21e878865d97b3a4d4afdecdd4e1cff45a0dc9d18efddb3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>Circular Dichroism</topic><topic>Computer Simulation</topic><topic>Magnetic Resonance Spectroscopy</topic><topic>Models, Chemical</topic><topic>Molecular Structure</topic><topic>Peptides - chemical synthesis</topic><topic>Peptides - chemistry</topic><topic>Protein Structure, Secondary</topic><topic>Temperature</topic><topic>Thermodynamics</topic><topic>Water - chemistry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Job, Gabriel E</creatorcontrib><creatorcontrib>Kennedy, Robert J</creatorcontrib><creatorcontrib>Heitmann, Björn</creatorcontrib><creatorcontrib>Miller, Justin S</creatorcontrib><creatorcontrib>Walker, Sharon M</creatorcontrib><creatorcontrib>Kemp, Daniel S</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of the American Chemical Society</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Job, Gabriel E</au><au>Kennedy, Robert J</au><au>Heitmann, Björn</au><au>Miller, Justin S</au><au>Walker, Sharon M</au><au>Kemp, Daniel S</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Temperature- and length-dependent energetics of formation for polyalanine helices in water: assignment of w(Ala)(n,T) and temperature-dependent CD ellipticity standards</atitle><jtitle>Journal of the American Chemical Society</jtitle><addtitle>J Am Chem Soc</addtitle><date>2006-06-28</date><risdate>2006</risdate><volume>128</volume><issue>25</issue><spage>8227</spage><epage>8233</epage><pages>8227-8233</pages><issn>0002-7863</issn><abstract>Length-dependent helical propensities w(Ala)(n,T) at T = 10, 25, and 60 degrees C are assigned from t/c values and NMR 13C chemical shifts for series 1 peptides TrpLys(m)Inp2(t)Leu-Ala(n)(t)LeuInp2Lys(m)NH2, n = 15, 19, and 25, m = 5, in water. Van't Hoff analysis of w(Ala)(n,T) show that alpha-helix formation is primarily enthalpy-driven. For series 2 peptides Ac-Trp Lys5Inp2(t)Leu-(beta)AspHel-Ala(n)-beta-(t)LeuInp2Lys5NH2, n = 12 and 22, which contain exceptionally helical Ala(n) cores, protection factor-derived fractional helicities FH are assigned in the range 10-30 degrees C in water and used to calibrate temperature-dependent CD ellipticities [theta](lambda,H,n,T). These are applied to CD data for series 1 peptides, 12 < or = n < or = 45, to confirm the w(Ala)(n,T) assignments at T = 25 and 60 degrees C. The [theta](lambda,H,n,T) are temperature dependent within the wavelength region, 222 +/- 12 nm, and yield a temperature correction for calculation of FH from experimental values of [theta](222,n,T,Exp).</abstract><cop>United States</cop><pmid>16787087</pmid><doi>10.1021/ja060094y</doi><tpages>7</tpages></addata></record> |
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| subjects | Circular Dichroism Computer Simulation Magnetic Resonance Spectroscopy Models, Chemical Molecular Structure Peptides - chemical synthesis Peptides - chemistry Protein Structure, Secondary Temperature Thermodynamics Water - chemistry |
| title | Temperature- and length-dependent energetics of formation for polyalanine helices in water: assignment of w(Ala)(n,T) and temperature-dependent CD ellipticity standards |
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