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Relative strength of cation-pi vs salt-bridge interactions: the Gtalpha(340-350) peptide/rhodopsin system.

Relative strength of cation-pi vs salt-bridge interactions: the Gtalpha(340-350) peptide/rhodopsin system. Research Abstract Details 

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  • Relative strength of cation-pi vs salt-bridge interactions: the Gtalpha(340-350) peptide/rhodopsin system. Abstract Text:

    matthew a andersonMatthew A Anderson,benhur ogbayBenhur Ogbay,rieko arimotoRieko Arimoto,wei shaWei Sha,oleg g kisselevOleg G Kisselev,david p cistolaDavid P Cistola,garland r marshallGarland R Marshall,

    Interactions between cationic and aromatic side chains of amino acid residues, the so-called cation-pi interaction, are thought to contribute to the overall stability of the folded structure of peptides and proteins. The transferred NOE NMR structure of the G(t)alpha(340-350) peptide bound to photoactivated rhodopsin (R*) geometrically suggests a cation-pi interaction stabilizing the structure between the epsilon-amine of Lys341 and the aromatic ring of the C-terminal residue, Phe350. This interaction has been explored by varying substituents on the phenyl ring to alter the electron density of the aromatic ring of Phe350 and observing the impact on binding of the peptide to R*. The results suggest that while a cation-pi interaction geometrically exists in the G(t)alpha(340-350) peptide when bound to R*, its energetic contribution to the stability of the receptor-bound structure is relatively insignificant, as it was not observed experimentally. The presence of an adjacent and competing salt-bridge interaction between the epsilon-amine of Lys341 and the C-terminal carboxylate of Phe350 effectively shields the charge of the ammonium group. Experimental data supporting a significant cation-pi interaction can be regained through a series of Phe350 analogues where the C-terminal carboxyl has been converted to the neutral carboxamide, thus eliminating the shielding salt-bridge. TrNOE NMR experiments confirmed the existence of the cation-pi interaction in the carboxamide analogues. Various literature estimates of the strength of cation-pi interactions, including some that estimate strengths in excess of salt-bridges, are compromised by omission of the relevant anion in the calculations.

    Relative strength of cation-pi vs salt-bridge interactions: the Gtalpha(340-350) peptide/rhodopsin system. Publishing Authors By Initials

    ma andersonMA Anderson,b ogbayB Ogbay,r arimotoR Arimoto,w shaW Sha,og kisselevOG Kisselev,dp cistolaDP Cistola,gr marshallGR Marshall,

    For similar inorganic chemicals: salts research abstracts see: inorganic chemicals: salts research

    PUBMED ID PMID:

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    Relative strength of cation-pi vs salt-bridge interactions: the Gtalpha(340-350) peptide/rhodopsin system. Journal Published:

    PUBLICATION TYPE: Research Support, Non-U.S. Gov

    Journal: Journal of the American Chemical Society

    VOLUME: 128

    Page Numbers: 7531-41

    Journal Abbreviation: J. Am. Chem. Soc.

    ISSN: 0002-7863

    DAY: 14

    MONTH: Jun

    YEAR: 2006

    Relative strength of cation-pi vs salt-bridge interactions: the Gtalpha(340-350) peptide/rhodopsin system. Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 7503056

    Relative strength of cation-pi vs salt-bridge interactions: the Gtalpha(340-350) peptide/rhodopsin system. Keywords Mesh Terms:

    KEYWORDS: Salts

    MESH TERMS: chemistry

    Chemical & Substance for Abstract: Relative strength of cation-pi vs salt-bridge interactions: the Gtalpha(340-350) peptide/rhodopsin system. Information

    Substance Name: Rhodopsin

    Registry Number: 9009-81-8

    Grant and Affiliation Information for Relative strength of cation-pi vs salt-bridge interactions: the Gtalpha(340-350) peptide/rhodopsin system.

    AFFILIATION: Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, Missouri 63110, USA.

    Country: United States

    United States Research PublicationUnited States Research Publication

    AGENCY: United States NCRR

    GRANT: P41RR00954

    ACRONYM: RR

    MEDLINETA: J Am Chem Soc

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    ACCESSION NUMBER:

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