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Force data are analyzed with a freely jointed chain model to extract effective Kuhn segment lengths linked to hydrophobic hydration behavior. Results qualitatively match molecular dynamics predictions and support hydrophobic hydration as a key contributor to ELP elasticity, enabling study of subtle polypeptide-water interactions.",{"@graph":14,"@context":73},[15,34,56],{"@type":16,"itemListElement":17},"BreadcrumbList",[18,23,27,31],{"item":19,"name":20,"@type":21,"position":22},"https://docshare.wps.com","Home","ListItem",1,{"item":24,"name":25,"@type":21,"position":26},"https://docshare.wps.com/document/","Document",2,{"item":28,"name":29,"@type":21,"position":30},"https://docshare.wps.com/document/research-report/","Research & 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variables affect the force-extension behavior of single, end-tethered elastin-like polypeptides (ELPs)?","Question",{"text":63,"@type":64},"Temperature, ionic strength, solvent polarity, and the type of guest residue are investigated as the main factors shaping the force-extension response.","Answer",{"name":66,"@type":61,"acceptedAnswer":67},"How are the force-extension data analyzed in the study?",{"text":68,"@type":64},"The data are fitted with a freely jointed chain (FJC) model to resolve differences in effective Kuhn segment length distributions related to hydrophobic hydration behavior.",{"name":70,"@type":61,"acceptedAnswer":71},"Why is hydrophobic hydration considered important for ELP elasticity?",{"text":72,"@type":64},"The study finds that the observed mechanical effects agree with molecular dynamics expectations and indicate that hydrophobic hydration contributes meaningfully to molecular elasticity in 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Chemical Society  \nHydration and Conformational Mechanics of Single End-Tethered Elastin  \nLike Polypeptides  \n\n| Journal: | Journal of the American Chemical Society |\n| --- | --- |\n| Manuscript ID: | ja-2008-00502h |\n| Manuscript Type: | Article |\n| Date Submitted by the Author: | 21-Jan-2008 |\n| Complete List of Authors: | Valiaev, Alexei; Duke University, Mechanical Engineering and Materials Science\u003Cbr>Lim, Dong Woo; Duke University, Biomedical Engineering Schmidler, Scott; Duke University, Statistics and Decision Sciences Clark, Robert; Duke University, Mechanical Engineering and Materials Science\u003Cbr>Chilkoti, Ashutosh; Duke University, Biomedical Engineering Zauscher, Stefan; Duke University, Mechanical Engineering and Materials Science |\n|  |  |\n\nACS Paragon Plus Environment  \nPage 1 of 31 Submitted to Journal of the American Chemical Society  \n1  \n2 3  \n4 5  \n6 7  \n8 9  \n10  \n11  \n12  \n13  \n14  \n15  \n16  \n17  \n18  \n19  \n20  \n21  \n22  \n23  \n24  \n25  \n26  \n27  \n28  \n29  \n30  \n31  \n32  \n33  \n34  \n35  \n36  \n37  \n38  \n39  \n40  \n41  \n42  \n43  \n44  \n45  \n46  \n47  \n48  \n49  \n50  \n51  \n52  \n53  \n54  \n55  \n56  \n57  \n58  \n59  \n60  \nHydration and Conformational Mechanics of Single End-Tethered Elastin-Like Polypeptides  \nAlexei Valiaev1,3, Dong Woo Lim2,3, Scott Schmidler4,Robert L. Clark1,3, Ashutosh Chilkoti2,3,  \nStefan Zauscher1,3*  \n1Duke University, Department of Mechanical Engineering and Materials Science  \n2Duke University, Department of Biomedical Engineering  \n3Center for Biologically Inspired Materials and Materials Systems  \n4Institute of Statistics and Decision Sciences  \nAUTHOR EMAIL ADDRESS: [zauscher@duke.edu](zauscher@duke.edu)  \nCORRESPONDING AUTHOR FOOTNOTE Send Correspondence to: Stefan Zauscher, Duke University, 144 Hudson Hall, Durham, NC 27708, e-mail: [zauscher@duke.edu](zauscher@duke.edu), Tel.:1 919 660- 5360  \nACS Paragon Plus Environment 1  \nSubmitted to Journal of the American Chemical Society Page 2 of 31  \n1  \n2 3  \n4 5  \n6 7  \n8 9  \n10  \n11  \n12  \n13  \n14  \n15  \n16  \n17  \n18  \n19  \n20  \n21  \n22  \n23  \n24  \n25  \n26  \n27  \n28  \n29  \n30  \n31  \n32  \n33  \n34  \n35  \n36  \n37  \n38  \n39  \n40  \n41  \n42  \n43  \n44  \n45  \n46  \n47  \n48  \n49  \n50  \n51  \n52  \n53  \n54  \n55  \n56  \n57  \n58  \n59  \n60  \nABSTRACT  \nWe investigated the effect of temperature, ionic strength, solvent polarity, and type of guest residue on the force-extension behavior of single, end-tethered elastin-like polypeptides (ELPs), using single molecule force spectroscopy (SMFS) . ELPs are stimulus-responsive polypeptides that contain repeats of the five amino acids Val-Pro-Gly-Xaa-Gly (VPGXG), where Xaa is a guest residue that can be any amino acid with the exception of proline. We fitted the forceextension data with a freely jointed chain (FJC) model which allowed us to resolve small differences in the effective Kuhn segment length distributions that largely arise from differences in the hydrophobic hydration behavior of ELP. Our results agree qualitatively with predictions from recent molecular dynamics simulations, and demonstrate that hydrophobic hydration is an important contributor to molecular elasticity for ELPs. Furthermore, our results show that SMFS, when combined with our approach for data analysis, can be used to study the subtleties of polypeptide-water interactions, and thus provides a basis for the study of hydrophobic hydration in intrinsically unstructured biomacromolecules.  \nKeywords: AFM force spectroscopy, stimulus-responsive polymers, single molecule, freelyjointed chain (FJC), 􀀁-spiral  \nACS Paragon Plus Environment 2  \nPage 3 of 31 Submitted to Journal of the American Chemical Society  \n1  \n2 3  \n4 5  \n6 7  \n8 9  \n10  \n11  \n12  \n13  \n14  \n15  \n16  \n17  \n18  \n19  \n20  \n21  \n22  \n23  \n24  \n25  \n26  \n27  \n28  \n29  \n30  \n31  \n32  \n33  \n34  \n35  \n36  \n37  \n38  \n39  \n40  \n41  \n42  \n43  \n44  \n45  \n46  \n47  \n48  \n49  \n50  \n51  \n52  \n53  \n54  \n55  \n56  \n57  \n58  \n59  \n60  \nINTRODUCTION  \nHydrati","cbCaipCD22pKe1Mf","https://ap.wps.com/l/cbCaipCD22pKe1Mf","pdf",765350,32,"English","# Abstract\n## Introduction\n## Hydration and conformational mechanics","[{\"question\":\"What variables affect the force-extension behavior of single, end-tethered elastin-like polypeptides (ELPs)?\",\"answer\":\"Temperature, ionic strength, solvent polarity, and the type of guest residue are investigated as the main factors shaping the force-extension response.\"},{\"question\":\"How are the force-extension data analyzed in the study?\",\"answer\":\"The data are fitted with a freely jointed chain (FJC) model to resolve differences in effective Kuhn segment length distributions related to hydrophobic hydration behavior.\"},{\"question\":\"Why is hydrophobic hydration considered important for ELP elasticity?\",\"answer\":\"The study finds that the observed mechanical effects agree with molecular dynamics expectations and indicate that hydrophobic hydration contributes meaningfully to molecular elasticity in ELPs.\"}]","Hydration and Conformational Mechanics of Single End-Tethered Elastin-Like Polypeptides - Article Abstract | PDF",1789998914,81]