Abstract:What is the smallest protein? This is actually not such a simple question to answer, because there is no established consensus among scientists as to the definition of a protein. We describe here a designed molecule consisting of only 10 amino acids. Despite its small size, its essential characteristics, revealed by its crystal structure, solution structure, thermal stability, free energy surface, and folding pathway network, are consistent with the properties of natural proteins. The existence of this kind of molecule deepens our understanding of proteins and impels us to define an "ideal protein" without inquiring whether the molecule actually occurs in nature.

The spin-lattice relaxation times, T1, of H217O have been measured for aqueous solutions of 2 di-, 2 trisaccharides, α-, and γ-c clodextrins as a function of the concentration at 25°C. The dynamic hydration numbers, nDHN, for 17 sugars including monosaccharides were expressed by the linear relation of the mean number of the equatorial OH groups. The second virial coefficients showed a good correlation with nDHN. Though the rotational correlation times, τch, of water molecules in the cosphere of sugar molecules increased with increasing the number of equatorial OH groups for monosaccharides, those for trisaccharides and cyclodextrins showed almost constant values. The relation between the values of the limiting diffusion coefficients and nDHN for sugars was found to be expressed by two lines with a large negative slope for mono- and di- saccharides, and a small negative slope for trisaccharides and cyclodextrins.

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