Abstract
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.
Original language | English |
---|---|
Pages (from-to) | 365-369 |
Number of pages | 5 |
Journal | Il Nuovo Cimento D |
Volume | 18 |
Issue number | 2-3 |
DOIs | |
State | Published - Feb 1996 |
Keywords
- 01.30.Cc
- 76.80
- 78.35
- 87.15.He
- Brillouin and Rayleigh scattering
- Conference proceedings
- Molecular dynamics and conformational changes
- Mössbauer effect
- other light scattering
- other γ-ray spectroscopy