12 research outputs found
Reentrant Melting of RNA with Quenched Sequence Randomness
The effect of quenched sequence disorder on the thermodynamics of RNA
secondary structure formation is investigated for two- and four-letter
alphabet models using the constrained annealing approach, from which the
temperature behavior of the free energy, specific heat, and helicity is
analytically obtained. For competing base pairing energies, the calculations
reveal reentrant melting at low temperatures, in excellent agreement with
numerical results. Our results suggest an additional mechanism for the
experimental phenomenon of RNA cold denaturation
Microscopic formulation of the Zimm-Bragg model for the helix-coil transition
A microscopic spin model is proposed for the phenomenological Zimm-Bragg
model for the helix-coil transition in biopolymers. This model is shown to
provide the same thermophysical properties of the original Zimm-Bragg model and
it allows a very convenient framework to compute statistical quantities.
Physical origins of this spin model are made transparent by an exact mapping
into a one-dimensional Ising model with an external field. However, the
dependence on temperature of the reduced external field turns out to differ
from the standard one-dimensional Ising model and hence it gives rise to
different thermophysical properties, despite the exact mapping connecting them.
We discuss how this point has been frequently overlooked in the recent
literature.Comment: 11 pages, 2 figure
Competition for hydrogen bond formation in the helix-coil transition and protein folding
The problem of the helix-coil transition of biopolymers in explicit solvents,
like water, with the ability for hydrogen bonding with solvent is addressed
analytically using a suitably modified version of the Generalized Model of
Polypeptide Chains. Besides the regular helix-coil transition, an additional
coil-helix or reentrant transition is also found at lower temperatures. The
reentrant transition arises due to competition between polymer-polymer and
polymer-water hydrogen bonds. The balance between the two types of hydrogen
bonding can be shifted to either direction through changes not only in
temperature, but also by pressure, mechanical force, osmotic stress or other
external influences. Both polypeptides and polynucleotides are considered
within a unified formalism. Our approach provides an explanation of the
experimental difficulty of observing the reentrant transition with pressure;
and underscores the advantage of pulling experiments for studies of DNA.
Results are discussed and compared with those reported in a number of recent
publications with which a significant level of agreement is obtained.Comment: 21 pages, 3 figures, submitted to Phys Rev
Collapse and hybridization of RNA: View from replica technique approach
The replica technique method is applied to investigate the kinetic behavior of the coarse-grained model for the RNA molecule. A non-equilibrium phase transition of second order between the glassy phase and the ensemble of freely fluctuating structures has been observed. The non-equilibrium steady state is investigated as well and the thermodynamic characteristics of the system have been evaluated. The non-equilibrium behavior of the specific heat is discussed. Based on our analysis, we point out the state in the kinetic pathway in which the RNA molecule is most prone to hybridization
Unified description of solvent effects in helix-coil transition
We analyze the problem of the helix-coil transition in explicit solvents analytically by using spin-based models incorporating two different mechanisms of solvent action: explicit solvent action through the formation of solvent-polymer hydrogen bonds that can compete with the intrinsic intra-polymer hydrogen bonded configurations (competing interactions) and implicit solvent action, where the solvent-polymer interactions tune biopolymer configurations by changing the activity of the solvent (non-competing interactions). The overall spin Hamiltonian is comprised of three terms: the background in vacuo Hamiltonian of the “Generalized Model of Polypeptide Chain” type and two additive terms that account for the two above mechanisms of solvent action. We show that on this level the solvent degrees of freedom can be explicitly and exactly traced over, the ensuing effective partition function combining all the solvent effects in a unified framework. In this way we are able to address helix-coil transitions for polypeptides, proteins, and DNA, with different buffers and different external constraints. Our spin-based effective Hamiltonian is applicable for treatment of such diverse phenomena as cold denaturation, effects of osmotic pressure on the cold and warm denaturation, complicated temperature dependence of the hydrophobic effect as well as providing a conceptual base for understanding the behavior of intrinsically disordered proteins and their analogues