We present a fast algorithm to search for repeating fragments within protein sequences. The technique is based on an extension of the Smith-Waterman algorithm that allows the calculation of sub-optimal alignments of a sequence against itself. We are able to estimate the statistical significance of a
Repeat sequence proteins as matrices for nanocomposites
β Scribed by Lawrence F. Drummy; Hilmar Koerner; David M. Phillips; Joseph C. McAuliffe; Manoj Kumar; B.L. Farmer; Richard A. Vaia; Rajesh R. Naik
- Publisher
- Elsevier Science
- Year
- 2009
- Tongue
- English
- Weight
- 744 KB
- Volume
- 29
- Category
- Article
- ISSN
- 0928-4931
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β¦ Synopsis
Recombinant protein-inorganic nanocomposites comprised of exfoliated Na + montmorillonite (MMT) in a recombinant protein matrix based on silk-like and elastin-like amino acid motifs (silk elastin-like protein (SELP)) were formed via a solution blending process. Charged residues along the protein backbone are shown to dominate long-range interactions, whereas the SELP repeat sequence leads to local protein/MMT compatibility. Up to a 50% increase in room temperature modulus and a comparable decrease in high temperature coefficient of thermal expansion occur for cast films containing 2-10 wt.% MMT.
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The sequence of two cDNA clones coding for the whole of the fl-subunit and most of the a-subunit of legumin are presented together with a considerable amount of protein sequence data to confirm the predicted amino acid sequence. A unique feature shown by these cDNAs is the presence of three 56 base