A piece in the puzzle of deciphering the antimicrobial properties of Histatin 5: The effect of chain length
A lack of stable tertiary structure characterizes IDPs under physiological conditions in vitro. It has been shown that ~30% of all proteins in eukaryotic organisms belong to this group and that IDPs are involved in many central biological processes and diseases. This discovery challenges the traditional protein structure paradigm, which states that a specific, well-defined structure is required for the correct function of a protein. Biochemical evidence has shown that IDPs are functional and that the lack of folded structure is related to function. The hypothesis is that IDPs adopt a structure upon adsorption to surfaces that give rise to a function. Hence, understanding how interactions with surfaces or membranes induce the secondary structure of IDPs will shed light on how IDPs perform their functions - that is a fundamental biology question. Here we aim to study the chain length that affects the peptide-membrane interactions by adding a tandem repeat of the Histatin 5 sequence and a peptide half of the chain (11-24). In both peptides, the percentage of histidines in the sequence is kept constant and the same as for Hst5 (29%).
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The recommended format for citing this dataset in a research publication is in the following format:
Marie Skepö; ERIKSSON SKOG Amanda; GERELLI YURI; GUTFREUND Philipp and Nicolò Paracini. (2023). A piece in the puzzle of deciphering the antimicrobial properties of Histatin 5: The effect of chain length. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.8-02-1007
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This data is not yet public
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