Interactions between hydrophobic side chains within α-helices
نویسندگان
چکیده
منابع مشابه
Interactions between amino acid side chains in cylindrical hydrophobic nanopores with applications to peptide stability.
Confinement effects on protein stability are relevant in a number of biological applications ranging from encapsulation in the cylindrical cavity of a chaperonin, translocation through pores, and structure formation in the exit tunnel of the ribosome. Consequently, free energies of interaction between amino acid side chains in restricted spaces can provide insights into factors that control pro...
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Using a new representation for interactions in protein sequences based on correlations between pairs of amino acids, we have examined α-helical segments from known protein structures for important interactions. Traditional techniques for representing protein sequences usually make an explicit assumption of conditional independence of residues in the sequences. Protein structure analyses, howeve...
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alpha-Helical transmembrane peptides, named WALP, with a hydrophobic sequence of leucine and alanine of varying length bordered at both ends by two tryptophans as membrane anchors, were synthesized to study the effect of hydrophobic matching in lipid bilayers. WALPs of 13-, 16-, and 19-residues were incorporated into 1,2-dilauroyl-sn-glycero-3-phosphocholine (12C), 1,2-tridecanoyl-sn-glycero-3-...
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Escherichia coli bacteria use rotating helical flagella to swim. At this scale, viscous effects dominate inertia, and there are significant hydrodynamic interactions between nearby helices. These interactions cause the flagella to bundle during the "runs" of bacterial chemotaxis. Here we use slender-body theory to solve for the flow fields generated by rigid helices rotated by stationary motors...
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Two designed peptide sequences containing Trp residues at positions i and i + 5 (Boc-Leu-Trp-Val-Ala-Aib-Leu-Trp-Val-OMe, 1) as well as i and i + 6 (Boc-Leu-Trp-Val-Aib-Ala-Aib-Leu-Trp-Val-OMe, 2) containing one and two centrally positioned Aib residues, respectively, for helix nucleation, have been shown to form stable helices in chloroform solutions. Structures derived from nuclear magnetic r...
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ژورنال
عنوان ژورنال: Protein Science
سال: 1995
ISSN: 0961-8368,1469-896X
DOI: 10.1002/pro.5560040706