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|Type:||Artigo de periódico|
|Title:||Anharmonic transitions in nearly dry L-cysteine I|
|Abstract:||Two special dynamical transitions of universal character have recently been observed in macromolecules (lysozyme, myoglobin, bacteriorhodopsin, DNA and RNA) at T* similar to 100-150 K and T-D similar to 180-220 K. The underlying mechanisms governing these transitions have been the subject of debate. In the present work, a survey is reported on the temperature dependence of structural, vibrational and thermodynamical properties of a nearly anhydrous amino acid (orthorhombic polymorph of the amino acid L-cysteine at a hydration level of 3.5%). The temperature dependence of x-ray powder diffraction patterns, Raman spectra and specific heat revealed these two transitions at T* = 70 K and T-D = 230 K for this sample. The data were analyzed considering amino acid-amino acid, amino acid-water, water-water phonon-phonon interactions and molecular rotor activation. Our results indicated that the two referred temperatures define the triggering of very simple and particular events that govern all the interactions of the biomolecular: activation of CH2 rigid rotors (T < T*), phonon-phonon interactions between specific amino acid and water dimer vibrational modes (T* < T < T-D), and water rotational barriers surpassing (T > T-D).|
|Editor:||Iop Publishing Ltd|
|Appears in Collections:||Unicamp - Artigos e Outros Documentos|
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