7.
Summary The classical model system poly-L-glutamic acid (poly-Glu), was investigated in a disordered coil state (at
pH=7.0) and in helix state (at
pH=2.0) by the RSMR technique. By considering that the coil state of poly-Glu models unfolded (random coil) state and α-helix
state models the fluctuating secondary structure (during consequent folding of protein), a comparative analysis of the dynamical
properties of poly-Glu in different states with the dynamical properties of different proteins in the native state (α-helical
myoglobin and HSA, partially β-sheet lysozyme) and in intermediate (molten globule) state (α-lactalbumin) was performed. This
comparison brings some unpredicted results: native α-helical proteins behave close to random coil, native partially β-sheet
proteins behave close to fluctuating secondary structure (α-helix) and the dynamic behaviour of molten-globule state (partially
β-sheet α-lactalbumin) is not different from the behaviour of lysozyme and much more rigid than that of native α-helical proteins.
Paper presented at ICAME-95, Rimini, 10–16 September 1995.
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