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Optimal attachment position and linker length promote native-like character of cavitand-based template-assembled synthetic proteins (TASPs).

Optimal attachment position and linker length promote native-like character of cavitand-based template-assembled synthetic proteins (TASPs). Research Abstract Details 

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  • Optimal attachment position and linker length promote native-like character of cavitand-based template-assembled synthetic proteins (TASPs). Abstract Text:

    emily s seoEmily S Seo,walter r p scottWalter R P Scott,suzana k strausSuzana K Straus,john c shermanJohn C Sherman,

    We have designed, synthesised and characterised a series of template-assembled de novo four-helix bundles, each differing in the linker length between the template and the peptides. The helix is based on an earlier peptide sequence: EELLKKLEELLKKLG (first-generation sequence), which was designed to link the hydrophilic/hydrophobic interface of the helices. Increasing or decreasing the linker length by one glycine residue had a significant effect on the structure and properties of the template-assembled synthetic proteins (TASPs). Here, the effect of the linker length is further probed by linking the peptides closer to the hydrophobic face by using the second-generation sequence, AEELLKKLEELLKKG, in an effort to improve the packing between the helices and to better understand the helical bundles. The peptides were synthesised with 0-4 Gly linker residues and linked onto a cavitand template. The proteins were found to be alpha-helical, stable to guanidine hydrochloride (GuHCl) and to unfold cooperatively. However, their stabilities toward GuHCl, propensity to self-aggregate and structural specificity differed. The two-glycine variant of the second-generation series demonstrated the highest stability and most native-like character of all the mononeric TASPs in both the first- and second-generation series. The structural specificity of this two glycine variant is comparable to that of other known native-like de novo proteins. Molecular dynamics simulations showed that the two-glycine variant contains helices that are tilted with respect to the cavitand template and may account for its unique properties.

    Optimal attachment position and linker length promote native-like character of cavitand-based template-assembled synthetic proteins (TASPs). Publishing Authors By Initials

    es seoES Seo,wr scottWR Scott,sk strausSK Straus,jc shermanJC Sherman,

    For similar biochemical phenomena, metabolism, and nutrition: biochemical phenomena: structure-activity relationship research abstracts see: biochemical phenomena, metabolism, and nutrition: biochemical phenomena: structure-activity relationship research

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    Optimal attachment position and linker length promote native-like character of cavitand-based template-assembled synthetic proteins (TASPs). Journal Published:

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

    Journal: Chemistry (Weinheim an der Bergstrasse, Germany)

    VOLUME: 13

    Page Numbers: 3596-605

    Journal Abbreviation:

    ISSN: 0947-6539

    DAY: 3

    MONTH: 12

    YEAR: 2007

    Optimal attachment position and linker length promote native-like character of cavitand-based template-assembled synthetic proteins (TASPs). Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 9513783

    Optimal attachment position and linker length promote native-like character of cavitand-based template-assembled synthetic proteins (TASPs). Keywords Mesh Terms:

    KEYWORDS: Structure-Activity Relationship

    MESH TERMS: chemistry

    Chemical & Substance for Abstract: Optimal attachment position and linker length promote native-like character of cavitand-based template-assembled synthetic proteins (TASPs). Information

    Substance Name: Guanidine

    Registry Number: 113-00-8

    Grant and Affiliation Information for Optimal attachment position and linker length promote native-like character of cavitand-based template-assembled synthetic proteins (TASPs).

    AFFILIATION: Department of Chemistry, University of British Columbia, 2036 Main Mall, Vancouver, BC, V6T 1Z1, Canada.

    Country: Germany

    Germany Research PublicationGermany Research Publication

    AGENCY: United States NCRR

    GRANT: P41 RR-01081

    ACRONYM: RR

    MEDLINETA: Chemistry

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    Optimal attachment position and linker length promote native-like character of cavitand-based template-assembled synthetic proteins TASPs Related Publications

     

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