Abstract
The intestinal fatty acid binding protein (IFABP) consists of ten β-strand fragments and two small α-helical fragments packed in a general β-sheet 3D structure (see the PDB entry HFC). This study presents the results of energy calculations for the isolated IFABP hexapeptide fragments 42–47 (G44), 62–67 (G65), 71–76 (G75), 84–89 (G86), 108–113 (G110) and 118–123 (G121), as well as for the same fragments in mutants obtained by the G/V mutations [1], The sets of low-energy conformers for these fragments may be regarded as the statistical ensembles of 3D structures accessible to the fragments during process of protein folding.
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© 2001 Springer Science+Business Media Dordrecht
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Nikiforovich, G.V., Frieden, C. (2001). Molecular Modeling Study of the β-Turn-Type Reversals Involved in 3D Structure of IFABP. In: Lebl, M., Houghten, R.A. (eds) Peptides: The Wave of the Future. American Peptide Symposia, vol 7. Springer, Dordrecht. https://doi.org/10.1007/978-94-010-0464-0_149
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DOI: https://doi.org/10.1007/978-94-010-0464-0_149
Publisher Name: Springer, Dordrecht
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