A Designed β-Hairpin Peptide for Molecular Recognition of ATP in Water
A designed 12-residue β-hairpin peptide with a diagonal tryptophan (Trp) pair was shown to bind ATP in water through a combination of aromatic and electrostatic interactions. The affinity for ATP was 5800 M-1 (ΔG ≈ −5.0 kcal/mol), a remarkable affinity for a short, structured peptide in water, consi...
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| Veröffentlicht in: | Journal of the American Chemical Society 2003-08, Vol.125 (32), p.9580-9581 |
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| container_title | Journal of the American Chemical Society |
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| creator | Butterfield, Sara M Waters, Marcey L |
| description | A designed 12-residue β-hairpin peptide with a diagonal tryptophan (Trp) pair was shown to bind ATP in water through a combination of aromatic and electrostatic interactions. The affinity for ATP was 5800 M-1 (ΔG ≈ −5.0 kcal/mol), a remarkable affinity for a short, structured peptide in water, consisting of entirely natural amino acid residues. Proton NMR measurements indicate that the adenine ring of the nucleotide is intercalated between the diagonal tryptophans in the bound state. Delineation of the contributions to ATP binding to the hairpin suggest that aromatic interactions contribute approximately −1.8 kcal/mol, while individual electrostatic interactions involving the ATP phosphates and positively charged side chains of the hairpin contribute approximately −1 kcal/mol each. The designed β-hairpin receptor presents a novel minimalist system to investigate the energetic contributions to protein−nucleic acid recognition through the surface of a β-sheet. |
| doi_str_mv | 10.1021/ja0359254 |
| format | Article |
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Am. Chem. Soc</addtitle><description>A designed 12-residue β-hairpin peptide with a diagonal tryptophan (Trp) pair was shown to bind ATP in water through a combination of aromatic and electrostatic interactions. The affinity for ATP was 5800 M-1 (ΔG ≈ −5.0 kcal/mol), a remarkable affinity for a short, structured peptide in water, consisting of entirely natural amino acid residues. Proton NMR measurements indicate that the adenine ring of the nucleotide is intercalated between the diagonal tryptophans in the bound state. Delineation of the contributions to ATP binding to the hairpin suggest that aromatic interactions contribute approximately −1.8 kcal/mol, while individual electrostatic interactions involving the ATP phosphates and positively charged side chains of the hairpin contribute approximately −1 kcal/mol each. The designed β-hairpin receptor presents a novel minimalist system to investigate the energetic contributions to protein−nucleic acid recognition through the surface of a β-sheet.</description><subject>Adenosine Triphosphate - chemistry</subject><subject>Amino Acid Sequence</subject><subject>Biological and medical sciences</subject><subject>Chemistry</subject><subject>Exact sciences and technology</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>General and physical chemistry</subject><subject>In solution. Condensed state. Thin layers</subject><subject>Kinetics</subject><subject>Molecular biophysics</subject><subject>Oligopeptides - chemistry</subject><subject>Physico-chemical properties of biomolecules</subject><subject>Protein Conformation</subject><subject>Solution properties</subject><subject>Solutions</subject><subject>Thermodynamics</subject><subject>Water - chemistry</subject><issn>0002-7863</issn><issn>1520-5126</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpt0MFOGzEQBmCrApVAe-AFkC9U6mHBY6_X3mOUtAEEakTT9mg5Xhs5bNbB3pXgtfogfSZcJSIXTqPRfPo1-hE6BXIBhMLlShPGa8rLD2gEnJKCA60O0IgQQgshK3aEjlNa5bWkEj6iI6A1KQnACM3GeGqTf-hsg__9La60jxvf4bnd9L6x2IWI70JrzdDqiO-tCQ-d733ocHB4vJjjbP_o3sZP6NDpNtnPu3mCfn3_tphcFbc_ZteT8W2hmaj7won8kiSGC7CugVpUDZeSOkeXtKJGaGdoJUltWVWDlpBvS1cSvQTHoCacnaAv29xNDE-DTb1a-2Rs2-rOhiEpwXgpmKwz_LqFJoaUonVqE_1axxcFRP1vTb21lu3ZLnRYrm2zl7uaMjjfAZ2Mbl3UnfFp7zhhEkqWXbF1PvX2-e2u46OqBBNcLeY_Ff19M2XT2b0q97naJLUKQ-xyd-88-Aoh4YyS</recordid><startdate>20030813</startdate><enddate>20030813</enddate><creator>Butterfield, Sara M</creator><creator>Waters, Marcey L</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>7X8</scope></search><sort><creationdate>20030813</creationdate><title>A Designed β-Hairpin Peptide for Molecular Recognition of ATP in Water</title><author>Butterfield, Sara M ; Waters, Marcey L</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a379t-f700280c571efd1976d5882ff2b262c7afc26809e3691a81882bf40ab1f319053</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>Adenosine Triphosphate - chemistry</topic><topic>Amino Acid Sequence</topic><topic>Biological and medical sciences</topic><topic>Chemistry</topic><topic>Exact sciences and technology</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>General and physical chemistry</topic><topic>In solution. Condensed state. Thin layers</topic><topic>Kinetics</topic><topic>Molecular biophysics</topic><topic>Oligopeptides - chemistry</topic><topic>Physico-chemical properties of biomolecules</topic><topic>Protein Conformation</topic><topic>Solution properties</topic><topic>Solutions</topic><topic>Thermodynamics</topic><topic>Water - chemistry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Butterfield, Sara M</creatorcontrib><creatorcontrib>Waters, Marcey L</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>MEDLINE - Academic</collection><jtitle>Journal of the American Chemical Society</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Butterfield, Sara M</au><au>Waters, Marcey L</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A Designed β-Hairpin Peptide for Molecular Recognition of ATP in Water</atitle><jtitle>Journal of the American Chemical Society</jtitle><addtitle>J. Am. Chem. Soc</addtitle><date>2003-08-13</date><risdate>2003</risdate><volume>125</volume><issue>32</issue><spage>9580</spage><epage>9581</epage><pages>9580-9581</pages><issn>0002-7863</issn><eissn>1520-5126</eissn><coden>JACSAT</coden><abstract>A designed 12-residue β-hairpin peptide with a diagonal tryptophan (Trp) pair was shown to bind ATP in water through a combination of aromatic and electrostatic interactions. The affinity for ATP was 5800 M-1 (ΔG ≈ −5.0 kcal/mol), a remarkable affinity for a short, structured peptide in water, consisting of entirely natural amino acid residues. Proton NMR measurements indicate that the adenine ring of the nucleotide is intercalated between the diagonal tryptophans in the bound state. 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| source | ACS Publications; MEDLINE |
| subjects | Adenosine Triphosphate - chemistry Amino Acid Sequence Biological and medical sciences Chemistry Exact sciences and technology Fundamental and applied biological sciences. Psychology General and physical chemistry In solution. Condensed state. Thin layers Kinetics Molecular biophysics Oligopeptides - chemistry Physico-chemical properties of biomolecules Protein Conformation Solution properties Solutions Thermodynamics Water - chemistry |
| title | A Designed β-Hairpin Peptide for Molecular Recognition of ATP in Water |
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