arXiv subjects

Yong-Yun Ji

Publications and source records attributed to Yong-Yun Ji.

4 recordsLinked to original sources

arXiv2019

Quantum Intelligence on Protein Folding Pathways

We study the protein folding problem on the base of the quantum approach we proposed recently by considering the model of protein chain with nine amino-acid residues. We introduced the concept of distance space and its projections on a $XY$-plane, and two characteristic quantities, one is called compactness of protein structure and another is called probability ratio involving shortest path. Our results not only confirmed the fast quantum folding time but also unveiled the existence of quantum intelligence hidden behind in choosing protein folding pathways.

physics.bio-ph↗

arXiv2005

The prion-like folding behavior in aggregated proteins

We investigate the folding behavior of protein sequences by numerically studying all sequences with maximally compact lattice model through exhaustive enumeration. We get the prion-like behavior of protein folding. Individual proteins remaining stable in the isolated native state may change their conformations when they aggregate. We observe the folding properties as the interfacial interaction strength changes, and find that the strength must be strong enough before the propagation of the most stable structures happens.

q-bio.BM↗

arXiv2004

The Role of Chaos in One-Dimensional Heat Conductivity

We investigate the heat conduction in a quasi 1-D gas model with various degree of chaos. Our calculations indicate that the heat conductivity $κ$ is independent of system size when the chaos of the channel is strong enough. The different diffusion behaviors for the cases of chaotic and non-chaotic channels are also studied. The numerical results of divergent exponent $α$ of heat conduction and diffusion exponent $β$ are in consistent with the formula $α=2-2/β$. We explore the temperature profiles numerically and analytically, which show that the temperature jump is primarily attributed to superdiffusion for both non-chaotic and chaotic cases, and for the latter case of superdiffusion the finite-size affects the value of $β$ remarkably.

cond-mat.dis-nn↗

arXiv2004

Medium effects on the selection of sequences folding into stable proteins in a simple model

We study the medium effects on the selection of sequences in protein folding by taking account of the surface potential in HP-model. Our analysis on the proportion of H and P monomers in the sequences gives a direct interpretation that the lowly designable structures possess small average gap. The numerical calculation by means of our model exhibits that the surface potential enhances the average gap of highly designable structures. It also shows that a most stable structure may be no longer the most stable one if the medium parameters changed.

q-bio.BM↗