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Please use this identifier to cite or link to this item: http://etd.iisc.ernet.in/2005/331

Title: De Novo Design Of Protein Secondary And Super Secondary Structural Elements: Investigation Of Interaction Patterns From The Crystal Structure Analysis Of Oligopeptides Containing α,β-Dehydrophenylalanine Crystal Structure Analysis Of Double Mutant M37L, P40S Thioredoxin From E.Coli
Authors: Rudresh, *
Advisors: Ramakumar, S
Keywords: Proteins - Design
alpha, Beta-dehydrophenylalanine
Escheirchia Coli
Peptide Crystallography
Peptides - Crystal Structure
Glycine Zipper Motif
Helical Hairpin Motif
Hairpin Eicosapeptide
De Novo Design
Submitted Date: May-2006
Abstract: ΔPhe an analogue of a coded amino acid phenylalanine (Phe) residue but with double bond between Cα and Cβ atoms, is one of the well studied residue among all the dehydro amino acids, as a conformation constraining amino acid. Due to the presence of double bond Cα=Cβ, and consequent conjugation of ΔPhe ring electrons with Cα=Cβ double bond, ΔPhe gains conformation restricting (constraining) characteristics compared to coded amino acid Phe. ΔPhe which assumes an achiral residue has all its atoms restricted to an approximate plane. Apart from the conformation constraining property, the designer friendly ΔPhe residue has its ability to i) engage in side chain aromatic interactions ii) act as nuclei for C-HLO/N-HLπ weak interactions involving the side chain and/ or backbone atoms, and iii) acquire ambidextrous conformation as observed in many model peptides. It is these properties, which makes ΔPhe, a residue of intense research in the field of de novo protein secondary and super secondary design. Analysis of solid state and solution state structures of containing ΔPhe residues suggests that ΔPhe, in general induces β-bend in short peptides and 310-helical conformation in longer peptides (>4).
URI: http://etd.iisc.ernet.in/handle/2005/331
Appears in Collections:Physics (physics)

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