A contact map is a key factor representing a specific protein structure. To simplify the protein contact map prediction, we predict the inter-residue contact clusters centred at the groups of their surrounding inter-residue contacts. In this paper, we adopt a Support Vector Machine (SVM)-based approach to predict the inter-residue contact cluster centres. The input of the SVM predictor includes sequence profile, evolutionary rate and predicted secondary structure. The SVM predictor is based on hydrophobic cores that may be considered as locations of the inter-residue contact clusters. About 35% of clustering centres of inter-residue contacts can be predicted accurately.
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http://dx.doi.org/10.1504/ijdmb.2010.037549 | DOI Listing |
Bioinformatics
November 2024
LAAS-CNRS, Université de Toulouse, CNRS, 31400 Toulouse, France.
Motivation: Characterizing the structure of flexible proteins, particularly within the realm of intrinsic disorder, presents a formidable challenge due to their high conformational variability. Currently, their structural representation relies on (possibly large) conformational ensembles derived from a combination of experimental and computational methods. The detailed structural analysis of these ensembles is a difficult task, for which existing tools have limited effectiveness.
View Article and Find Full Text PDFJ Chem Theory Comput
September 2024
Department of Chemistry, University of Warwick, Coventry CV4 7AL, U.K.
We have recently shown how physically realizable protein-folding pathways can be generated using directed walks in the space of inter-residue contact-maps; combined with a back-transformation to move from protein contact-maps to Cartesian coordinates, we have demonstrated how this approach can generate protein-folding trajectory ensembles without recourse to molecular dynamics. In this article, we demonstrate that this framework can be used to study a challenging protein-folding problem that is known to exhibit two different folding paths which were previously identified through molecular dynamics simulation at several different temperatures. From the viewpoint of protein-folding mechanism prediction, this particular problem is extremely challenging to address, specifically involving folding to an identical nontrivial compact native structure along distinct pathways defined by heterogeneous secondary structural elements.
View Article and Find Full Text PDFJ Phys Chem B
September 2024
Graduate School of Science, Nagoya University, Furo-cho, Chikusa-ku, Nagoya 464-8602, Japan.
Within the protein interior, where we observe various types of interactions, nonuniform flow of thermal energy occurs along the polypeptide chain and through nonbonded native contacts, leading to inhomogeneous transport efficiencies from one site to another. The folded native protein serves not merely as thermal transfer medium but, more importantly, as sophisticated molecular nanomachines in cells. Therefore, we are particularly interested in what sort of "communication" is mediated through native contacts in the folded proteins and how such features are quantitatively depicted in terms of local transport coefficients of heat currents.
View Article and Find Full Text PDFJ Chem Phys
August 2024
Biomolecular Dynamics, Institute of Physics, University of Freiburg, 79104 Freiburg, Germany.
While the linear Pearson correlation coefficient represents a well-established normalized measure to quantify the inter-relation of two stochastic variables X and Y, it fails for multidimensional variables, such as Cartesian coordinates. Avoiding any assumption about the underlying data, the mutual information I(X, Y) does account for multidimensional correlations. However, unlike the normalized Pearson correlation, it has no upper bound (I ∈ [0, ∞)), i.
View Article and Find Full Text PDFJ Chem Theory Comput
October 2024
Department of Chemistry, Iowa State University, Ames, Iowa 50011, United States.
Decoding allostery at the atomic level is essential for understanding the relationship between a protein's sequence, structure, and dynamics. Recently, we have shown that decomposing temperature responses of inter-residue contacts can reveal allosteric couplings and provide useful insight into the functional dynamics of proteins. The details of this Chemically Accurate Contact Response Analysis (ChACRA) are presented here along with its application to two well-known allosteric proteins.
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