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Recent studies on protein folding explore various aspects such as kinetics, cooperativity, and computational strategies. Protein folding kinetics are linked to sequence-dependent properties, with folding times correlating to specific thermal measures. Additionally, cooperativity in protein folding is assessed using dimensionless measures, while novel Monte Carlo strategies, like the pruned-enriched Rosenbluth method, have shown efficiency in folding simulations. Moreover, solvable models are being used to identify crucial folding stages relevant to drug resistance, highlighting their potential in therapeutic applications.
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arxiv.org
Protein Folding Kinetics: Time Scales, Pathways, and Energy Landscapes in Terms of Sequence Dependent Properties

The folding kinetics of a number of sequences for off-lattice continuum model of proteins is studied using Langevin simulations at two values of the friction coefficient. We show that there is a remarkable correlation between folding times, $τ_{F}$, and $σ= (T_{θ} - T_{F})/T_{θ} $, where $T_{θ}…

cond-mat.stat-mech q-bio
arxiv.org
Cooperativity in Protein Folding: From Lattice Models with Side Chains to Real Proteins

We consider equilibrium folding transitions in lattice protein models with and without side chains. A dimensionless measure, $Omega_{c}$, is introduced to quantitatively assess the degree of cooperativity in lattice models and in real proteins. We show that larger values of $Ω_{c}$ resembling those…

cond-mat.soft q-bio
arxiv.org
Testing a New Monte Carlo Strategy for Folding Model Proteins

We demonstrate that the recently proposed pruned-enriched Rosenbluth method PERM (P.~Grassberger, Phys.~Rev.~{\bf E 56} (1997) 3682) leads to very efficient algorithms for the folding of simple model proteins. We test it on several models for lattice heteropolymers, and compare to published Monte …

cond-mat.soft q-bio
arxiv.org
Crucial stages of protein folding through a solvable model: predicting target sites for enzyme-inhibiting drugs

An exactly solvable model based on the topology of a protein native state is applied to identify bottlenecks and key-sites for the folding of HIV-1 Protease. The predicted sites are found to correlate well with clinical data on resistance to FDA-approved drugs. It has been observed that the effects …

cond-mat.stat-mech cond-mat.soft q-bio.BM
arxiv.org
mRNA Folding Algorithms for Structure and Codon Optimization

mRNA technology has revolutionized vaccine development, protein replacement therapies, and cancer immunotherapies, offering rapid production and precise control over sequence and efficacy. However, the inherent instability of mRNA poses significant challenges for drug storage and distribution, parti…

q-bio.BM q-bio.QM
arxiv.org
Two-phase protein folding optimization on a three-dimensional AB off-lattice model

This paper presents a two-phase protein folding optimization on a three-dimensional AB off-lattice model. The first phase is responsible for forming conformations with a good hydrophobic core or a set of compact hydrophobic amino acid positions. These conformations are forwarded to the second phase,…

cs.NE physics.comp-ph
arxiv.org
AlphaFold predicts the most complex protein knot and composite protein knots

The computer artificial intelligence system AlphaFold has recently predicted previously unknown three-dimensional structures of thousands of proteins. Focusing on the subset with high-confidence scores, we algorithmically analyze these predictions for cases where the protein backbone exhibits rare t…

q-bio.BM cond-mat.soft physics.bio-ph
arxiv.org
Localization of Energetic Frustration in Proteins

We present a detailed heuristic method to quantify the degree of local energetic frustration manifested by protein molecules. Current applications are realized in computational experiments where a protein structure is visualized highlighting the energetic conflicts or the concordance of the local in…

q-bio.BM