TAILIEUCHUNG - Báo cáo khoa học: Solubility-dependent structural formation of a 25-residue, natively unfolded protein, induced by addition of a seven-residue peptide fragment

To elucidate the architectural principle of protein structure, we focused on sequestration from solvent, which is a common characteristic of folding and self-associative precipitation. Because protein solubility can be regarded as a basis for the potential ability to sequester from solvent, we assume that poorly soluble proteins tend not only to precipitate, but also to form solution structures. | ễFEBS Journal Solubility-dependent structural formation of a 25-residue natively unfolded protein induced by addition of a seven-residue peptide fragment Mitsugu Araki and Atsuo Tamura Graduate Schoolof Science Kobe University Nada Japan Keywords folding intrinsically unstructured protein protein stability self-association solubility Correspondence A. Tamura Graduate School of Science Kobe University Nada Kobe 657-8501 Japan Fax Tel 81 78 803 5692 E-mail tamuatsu@ Database The atomic coordinates have been deposited in the Protein Data Bank PDB ID code 2KFQ for FP1 Received 26 September 2008 revised 10 February 2009 accepted 12 February 2009 doi To elucidate the architectural principle of protein structure we focused on sequestration from solvent which is a common characteristic of folding and self-associative precipitation. Because protein solubility can be regarded as a basis for the potential ability to sequester from solvent we assume that poorly soluble proteins tend not only to precipitate but also to form solution structures. To examine this the solubility of a 25-residue natively unfolded protein modified from a zinc-finger domain of transcription factor Sp1 was disturbed by adding a seven-residue hydrophobic peptide fragment to the C-terminus. NMR and ultracentrifuge measurements of the resulting sequence showed that a dissolved species forms an a-helical structure in a 15-20 molecule oligomer. To elucidate the mechanism by which the structure forms we prepared two variants in which the added fragments are less hydrophobic the structural stabilities were then measured at various pH values. A fairly good correlation was observed between stability and hydration potential whereas a much stronger correlation was observed between stability and solubility indicating that the stability is more strongly dependent on the ability to precipitate than on dehydration. These results show that among poorly soluble protein .

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