Results 11 to 20 of about 131,881 (286)

A Simple Model for the DNA Denaturation Transition [PDF]

open access: yesPhysical Review E, 1999
We study pairs of interacting self-avoiding walks on the 3d simple cubic lattice. They have a common origin and are allowed to overlap only at the same monomer position along the chain. The latter overlaps are indeed favored by an energetic gain.
A.M. Ferrenberg   +35 more
core   +4 more sources

Comment on "Why is the DNA denaturation transition first order?" [PDF]

open access: yesPhysical Review Letters, 2003
In this comment we argue that while the conclusions in the original paper (Y. Kafri, D. Mukamel and L. Peliti, Phys. Rev. Lett. 85, 4988 (2000)) are correct for asymptotically long DNA chains, they do not apply to the chains used in typical experiments ...
Andreas Hanke   +6 more
core   +5 more sources

RNA denaturation: excluded volume, pseudoknots and transition scenarios [PDF]

open access: yesPhysical Review Letters, 2003
A lattice model of RNA denaturation which fully accounts for the excluded volume effects among nucleotides is proposed. A numerical study shows that interactions forming pseudoknots must be included in order to get a sharp continuous transition ...
A. L. Stella   +12 more
core   +3 more sources

Order of the phase transition in models of DNA thermal denaturation [PDF]

open access: yesPhysical Review Letters, 2000
We examine the behavior of a model which describes the melting of double-stranded DNA chains. The model, with displacement-dependent stiffness constants and a Morse on-site potential, is analyzed numerically; depending on the stiffness parameter, it is ...
A. Campa   +25 more
core   +4 more sources

Renormalisation group determination of the order of the DNA denaturation transition [PDF]

open access: yesEPL (Europhysics Letters), 2010
We report on the nature of the thermal denaturation transition of homogeneous DNA as determined from a renormalisation group analysis of the Peyrard-Bishop-Dauxois model.
Dietrich S.   +14 more
core   +5 more sources

The denaturation transition of DNA in mixed solvents. [PDF]

open access: yesBiophys J, 2006
The helix-to-coil denaturation transition in DNA has been investigated in mixed solvents at high concentration using ultraviolet light absorption spectroscopy and small-angle neutron scattering. Two solvents have been used: water and ethylene glycol. The "melting" transition temperature was found to be 94 degrees C for 4% mass fraction DNA/d-water and ...
Hammouda B, Worcester D.
europepmc   +4 more sources

Pepsinogen denaturation is not a two‐state transition [PDF]

open access: yesFEBS Letters, 1981
1. introduction The knowledge of the mode of the denaturation reaction of proteins is important not only to under- stand their mechanism of folding, but also to obtain infomlation on their structural organization. From this point of view pepsinogen is one of the most inter- esting objects, since it is sufficiently large (M, 40 000) and its denaturation
Mateo, Pedro L., Privalov, Peter L.
openaire   +2 more sources

Disorder and denaturation transition in the generalized Poland–Scheraga model [PDF]

open access: yesAnnales Henri Lebesgue, 2020
We investigate the generalized Poland–Scheraga model, which is used in the bio-physical literature to model the DNA denaturation transition, in the case where the two strands are allowed to be non-complementary (and to have different lengths).
Quentin Berger   +2 more
openaire   +6 more sources

The dynamics of the DNA denaturation transition [PDF]

open access: yesEPL (Europhysics Letters), 2012
The dynamics of the DNA denaturation is studied using the Peyrard-Bishop-Dauxois model. The denaturation rate of double stranded polymers decreases exponentially as function of length below the denaturation temperature. Above Tc, the rate shows a minimum, but then increases as function of length.
van Erp, Titus S., Peyrard, Michel
openaire   +2 more sources

Polar or apolar--the role of polarity for urea-induced protein denaturation. [PDF]

open access: yesPLoS Computational Biology, 2008
Urea-induced protein denaturation is widely used to study protein folding and stability; however, the molecular mechanism and driving forces of this process are not yet fully understood.
Martin C Stumpe, Helmut Grubmüller
doaj   +1 more source

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