Force induced unfolding of biopolymers in a cellular environment: a model study.
نویسندگان
چکیده
Effect of molecular crowding and confinement experienced by protein in the cell during unfolding has been studied by modeling a linear polymer chain on a percolation cluster. It is known that internal structure of the cell changes in time, however, they do not change significantly from their initial structure. In order to model this we introduce the correlation among the different disorder realizations. It was shown that the force-extension behavior for correlated disorder in both constant force ensemble and constant distance ensemble is significantly different than the one obtained in absence of molecular crowding.
منابع مشابه
Weak temporal signals can synchronize and accelerate the transition dynamics of biopolymers under tension.
In addition to thermal noise, which is essential to promote conformational transitions in biopolymers, the cellular environment is replete with a spectrum of athermal fluctuations that are produced from a plethora of active processes. To understand the effect of athermal noise on biological processes, we studied how a small oscillatory force affects the thermally induced folding and unfolding t...
متن کاملSteered molecular dynamics simulations of force-induced protein domain unfolding.
Steered molecular dynamics (SMD), a computer simulation method for studying force-induced reactions in biopolymers, has been applied to investigate the response of protein domains to stretching apart of their terminal ends. The simulations mimic atomic force microscopy and optical tweezer experiments, but proceed on much shorter time scales. The simulations on different domains for 0.6 nanoseco...
متن کاملDistribution, Transition and Thermodynamic Stability of Protein Conformations in the Denaturant-Induced Unfolding of Proteins
BACKGROUND Extensive and intensive studies on the unfolding of proteins require appropriate theoretical model and parameter to clearly illustrate the feature and characteristic of the unfolding system. Over the past several decades, four approaches have been proposed to describe the interaction between proteins and denaturants, but some ambiguity and deviations usually occur in the explanation ...
متن کاملRole of conformational entropy in force-induced biopolymer unfolding.
A statistical mechanical description of flexible and semiflexible polymer chains in a poor solvent is developed in the constant force and constant distance ensembles. We predict the existence of many intermediate states at low temperatures stabilized by the force. A unified response to pulling and compressing forces has been obtained in the constant distance ensemble. We show the signature of a...
متن کاملManipulation of single molecules in biology.
The mechanical manipulation of single biological molecules is stimulating new and exciting research in many fields of study, including molecular motor mechanics, biopolymer properties, protein unfolding, receptor-ligand interactions, and more. Some recent highlights include the elucidation of the coupling ratios of myosin and kinesin, the demonstration of oscillatory forces in dynein arms, the ...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید
ثبت ناماگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید
ورودعنوان ژورنال:
- The Journal of chemical physics
دوره 131 6 شماره
صفحات -
تاریخ انتشار 2009