Role of the dihedral angle potential in the nucleation pathway of protein folding

Yuri S. Djikaev

Home/Archive/arXiv

arXiv · physics/0608252

Role of the dihedral angle potential in the nucleation pathway of protein folding

Yuri S. Djikaev

View original source ↗Read source document ↗Export metadata ↓

Abstract

A kinetic model for the nucleation mechanism of protein folding is proposed. A protein is modeled as a heteropolymer consisting of hydrophobic and hydrophilic beads with equal constant bond lengths and bond angles. The total energy of the heteropolymer is determined by the repulsive/attractive interactions of non-linked beads and the contribution from the dihedral angles involved. Their parameters can be rigorously defined, unlike the ill defined surface tension of a cluster of protein residues which is the basis of the previous model. As a crucial idea of the model, the dihedral potential in which a selected bead is involved is averaged over all possible configurations of neighboring beads along the protein chain. The resulting average dihedral potential of the residue is constant far enough from the cluster, but increases monotonically with decreasing distance below a threshold value. An overall potential around the cluster wherein a residue performs a chaotic motion is a combination of the average dihedral and pairwise potentials. As a function of distance from the cluster it has a double well shape. Residues in the inner well are considered as belonging to the cluster (folded part of the protein) while those in the outer well are treated as belonging to the unfolded (although compact) part of the protein. A double well shape of the potential around the cluster allows one to determine its emission and absorption rates by using a first passage time analysis and develop a self-consistent kinetic theory for the nucleation mechanism of protein folding. Numerical calculations for a protein of 2500 residues with the diffusion coefficient of residues in the native state ranging from 10^{-6} cm^2/s to 10^{-8} cm^2/s predict folding times in the range from several seconds to several hundreds of seconds.

Explore related subjects

physics.bio-ph physics.comp-ph

Keep this discovery

Explore connections, maps & timelines

BibTeX RIS

Yuri S. Djikaev. 2006-08-25. Role of the dihedral angle potential in the nucleation pathway of protein folding. https://arxiv.org/abs/physics/0608252

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related papers

arXiv2026

Tracking and distinguishing slime mold solutions to traveling salesperson problems through synchronized amplification in the non-equilibrium steady state

The plasmodium of the true slime mold Physarum polycephalum-an ancient, unicellular, aneural organism-serves as a platform for studying the information-processing capacities of active matter. Previous experiments used Physarum's intricate morphological dynamics and photoavoidance in stellate chips to solve $N$-city traveling salesperson problems (TSPs) of up to eight cities, scaling linearly in time with TSP size. Optical feedback controlled by a modified Hopfield network illuminated specific lanes at regular intervals, prompting Physarum to elongate or retract selected branches. When the illumination pattern stabilized in a non-equilibrium steady state, branches bifurcated reproducibly into solution and non-solution groups, with the former exhibiting lower-frequency, higher-amplitude, and more synchronized oscillations than the latter across 41 trials with valid TSP solutions. Physarum's synchronization dynamics efficiently predict 100% of selected solutions by the midpoint of the optical-feedback interval, achieving statistically significant (paired t-test, $p<0.005$) discrimination from alternate tours well before the non-equilibrium steady state. Observed frequency downconversions and synchronized power amplifications scale linearly and quadratically, respectively, for small-to-moderate TSP size, as captured by a toy model of energy redistribution with saturating optical absorption. Tuning these features in native biomolecular chromophore networks may thus improve both the quality and efficiency of TSP solutions from Physarum-based biocomputers, which exploit the effects of organismal-scale coherence.

physics.bio-ph↗

arXiv2026

How do incorrect ligands help detect a correct ligand?

Intrigued by the response of T cell receptors to the presence of a few agonist ligands, we propose a minimal model that can achieve similar performance. The model consists of a small cluster of immobile receptors that bind reversibly to two types (correct/incorrect) of ligands in the environment, with slightly weaker binding strength for the incorrect one. It features binding-state coupling between nearest-neighbor receptors, and receptors in the bound/free states are activated/deactivated by specific enzymes, with rates that allow kinetic proofreading. It is found that, for a range of binding-state coupling strength, incorrect ligands alone cannot activate the receptors, but the binding of merely one correct ligand to a receptor is sufficient to promote the activation of other receptors via induced binding to incorrect ligands. Both response time and signal amplification increase as the receptor binding-state coupling strength increases until it reaches an optimal range to achieve the most rapid and sensitive response. These results suggest a possible mechanism for a speedy and specific response of receptors to very few correct ligands in biological and artificial systems at the subcellular scale.

physics.bio-ph↗

arXiv2026

Coherence in Biological Systems

When does a collection of autonomous cells become a multicellular individual? We propose that coherence provides a physical description of this transition. Coherence is treated as a global property arising when distinguishable constituents admit a physically meaningful collective state-space description. Using the center of mass and an interaction-based construction, we show that such collective states can be defined for classical bodies before dynamics is introduced, with normal modes emerging as a particular dynamical realization. We apply this framework to multicellular organization, where cells retain their identities while their independent individuality is replaced by participation in the organized whole. In \emph{Dictyostelium discoideum}, cAMP-mediated coupling produces population-level collective modes, while starvation provides an experimentally controlled energetic constraint on the transition to multicellularity. The framework yields direct tests through interaction-derived collective eigenstates and the energetic cost of maintaining autonomous versus collective organization. Coherence may thus provide a general physical description of multicellular individuality without requiring microscopic quantum coherence or intrinsic wave character.

physics.bio-ph↗