By a News Reporter-Staff News Editor at Science Letter -- Current study results on Molecular Research have been published. According to news reporting from Ames, Iowa, by NewsRx journalists, research stated, "A common feature of biomineralization proteins is their self-assembly to produce a surface consistent in size with the inorganic crystals that they produce. Mms6, a small protein of 60 amino acids from Magnetospirillum magneticum strain AMB-1 that promotes the in vitro growth of superparamagnetic magnetite nanocrystals, assembles in aqueous solution to form spherical micelles that could be visualized by TEM and AFM."
The news correspondents obtained a quote from the research from Iowa State University, "The results reported here are consistent with the view that the N and C-terminal domains interact with each other within one polypeptide chain and across protein units in the assembly. From studies to determine the amino acid residues important for self-assembly, we identified the unique GL repeat in the N-terminal domain with additional contributions from amino acids in other positions, throughout the molecule. Analysis by CD spectroscopy identified a structural change in the iron-binding C-terminal domain in the presence of Fe3+. A change in the intrinsic fluorescence of tryptophan in the N-terminal domain showed that this structural change is transmitted through the protein."
According to the news reporters, the research concluded: "Thus, self-assembly of Mms6 involves an interlaced structure of intra-and inter-molecular interactions that results in a coordinated structural change in the protein assembly with iron binding."
For more information on this research see: Integrated Self-Assembly of the Mms6 Magnetosome Protein to Form an Iron-Responsive Structure. International Journal of Molecular Sciences, 2013;14(7):14594-14606. International Journal of Molecular Sciences can be contacted at: Mdpi Ag, Postfach, Ch-4005 Basel, Switzerland (see also Molecular Research).
Our news journalists report that additional information may be obtained by contacting S.R. Feng, Iowa State University, Dept. of Chem & Biol Engn, Ames, IA 50011, United States. Additional authors for this research include L.J. Wang, P. Palo, X.P. Liu, S.K. Mallapragada and M. Nilsen-Hamilton.
Keywords for this news article include: Ames, Iowa, United States, Molecular Research, North and Central America
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