75 research outputs found
Characteristic Temperatures of Folding of a Small Peptide
We perform a generalized-ensemble simulation of a small peptide taking the
interactions among all atoms into account. From this simulation we obtain
thermodynamic quantities over a wide range of temperatures. In particular, we
show that the folding of a small peptide is a multi-stage process associated
with two characteristic temperatures, the collapse temperature T_{\theta} and
the folding temperature T_f. Our results give supporting evidence for the
energy landscape picture and funnel concept. These ideas were previously
developed in the context of studies of simplified protein models, and here for
the first time checked in an all-atom Monte Carlo simulation.Comment: Latex, 6 Figure
Non-Markovian Configurational Diffusion and Reaction Coordinates for Protein Folding
The non-Markovian nature of polymer motions is accounted for in folding
kinetics, using frequency-dependent friction. Folding, like many other problems
in the physics of disordered systems, involves barrier crossing on a correlated
energy landscape. A variational transition state theory (VTST) that reduces to
the usual Bryngelson-Wolynes Kramers approach when the non-Markovian aspects
are neglected is used to obtain the rate, without making any assumptions
regarding the size of the barrier, or the memory time of the friction. The
transformation to collective variables dependent on the dynamics of the system
allows the theory to address the controversial issue of what are ``good''
reaction coordinates for folding.Comment: 9 pages RevTeX, 3 eps-figures included, submitted to PR
Molecular dynamics simulation of polymer helix formation using rigid-link methods
Molecular dynamics simulations are used to study structure formation in
simple model polymer chains that are subject to excluded volume and torsional
interactions. The changing conformations exhibited by chains of different
lengths under gradual cooling are followed until each reaches a state from
which no further change is possible. The interactions are chosen so that the
true ground state is a helix, and a high proportion of simulation runs succeed
in reaching this state; the fraction that manage to form defect-free helices is
a function of both chain length and cooling rate. In order to demonstrate
behavior analogous to the formation of protein tertiary structure, additional
attractive interactions are introduced into the model, leading to the
appearance of aligned, antiparallel helix pairs. The simulations employ a
computational approach that deals directly with the internal coordinates in a
recursive manner; this representation is able to maintain constant bond lengths
and angles without the necessity of treating them as an algebraic constraint
problem supplementary to the equations of motion.Comment: 15 pages, 14 figure
Base flipping in DNA: Pathways and energetics studied with molecular dynamic simulations
Carrying out chemistry on the bases of DNA, necessary for biological processes such as methylation or repair, requires flipping the base into an accessible position. In this work, molecular dynamics simulations are used to generate a free energy profile for flipping a cytosine base out of its helical stack in double-stranded DNA. The results shed light on the mechanics of this process by comparing routes for base flipping via the minor and major grooves
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