Quanta of local conformational change: conformons in α-helical proteins

  title={Quanta of local conformational change: conformons in $\alpha$-helical proteins},
  author={Victor Atanasov and Yasser Omar},
  journal={New Journal of Physics},
We propose the conformon as a quantum of local conformational change for energy transfer in α-helical proteins. The underlying mechanism of interaction between the quantum of excitation and the conformational degrees of freedom is nonlinear and leads to solitary wave packets of conformational energy. The phenomenon is specific to α-helices and not to β-sheets in proteins due to the three strands of hydrogen bonds constituting the α-helical backbone. 
4 Citations
Localization to delocalization transition in a double stranded helical geometry: effects of conformation, transverse electric field and dynamics
The interplay between the helical geometry and electric field may open up several notable features of electronic localization and can be verified by using different chiral molecules.
Quantum-elastic bump on a surface
We use an exact solution of the elastic membrane shape equation, representing the curvature, which will serve as a quantum potential in the quantum mechanical two dimensional Schrödinger equation for
Focus on quantum effects and noise in biomolecules
These examples show that the full understanding of the dynamics at bio-molecular length and timescales in noisy biological systems can uncover novel phenomena and concepts and hence present a fertile ground for truly multidisciplinary research.


Collective aspects of conformons and the electron transfer chain.
  • G. Kemeny
  • Physics, Chemistry
    Journal of theoretical biology
  • 1974
The structure of proteins; two hydrogen-bonded helical configurations of the polypeptide chain.
This work has used information about interatomic distances, bond angles, and other configurational parameters to construct two reasonable hydrogen-bonded helical configurations for the polypeptide chain; it is likely that these configurations constitute an important part of the structure of both fibrous and globular proteins, as well as of syntheticpolypeptides.
Quantum effective potential, electron transport and conformons in biopolymers
In the Kirchhoff model of a biopolymer, conformation dynamics can be described in terms of solitary waves, for certain special cross-section asymmetries. Applying this to the problem of electron
Long-Lived Amide I Vibrational Modes in Myoglobin
Pump-probe experiments in the infrared measure vibrational relaxation rates, suggesting that the alpha helix in proteins can support nonlinear states of 15 ps characteristic times.
Excited-state lifetimes of far-infrared collective modes in proteins.
The first direct measurement on the lifetime of vibrational excitations of the collective modes at 87 microm (115 cm(-1)) in bacteriorhodopsin, a transmembrane protein, is reported, suggesting that there is a connection between this relatively slow anharmonic relaxation rate and the similar observed rate of conformational transitions in proteins, which require multilevel vibrationalexcitations.
Tunneling pathway and redox-state-dependent electronic couplings at nearly fixed distance in electron transfer proteins
The tunneling pathway model for electron transfer, which accounts for the unique covalent, hydrogen-bonded, and van der Waals contact linking donor and acceptor in a protein, gives a consistent
Migration of small molecules through the structure of hemoglobin: evidence for gating in a protein electron-transfer reaction.
It was found that the activation energies for all three quenchers were very similar and closely resembled those in myoglobin, suggesting that the migration rates are determined by the subunit structure only and that the quaternary configurational changes do not influence the quenching rates.
Effect of conformations on charge transport in a thin elastic tube
We study the effect of conformations on charge transport in a thin elastic tube. Using the Kirchhoff model for a tube with any given Poisson ratio, cross-sectional shape and intrinsic twist, we