A new generation of statistical potentials for proteins.
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Summary
A novel and flexible derivation scheme of statistical, database-derived, potentials, which allows one to take simultaneously into account specific correlations between several sequence and structure descriptors, which leads to the decomposition of the total folding free energy of a protein into a sum of lower order terms.
- Type
- article
- Published
- 2006-06-01
- Cited by
- 123
- References
- 53
- Access
- Open access
- OpenAlex
- https://openalex.org/W2074002527
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:37053956
Keywords
Formalism (music), Computer science, Algorithm, Decoy, Chemistry
References
- Residue-residue potentials with a favorable contact pair term and an unfavorable high packing density term, for simulation and threading.
- What should the Z‐score of native protein structures be?
- Different derivations of knowledge-based potentials and analysis of their robustness and context-dependent predictive power.
- Pair potentials for protein folding: Choice of reference states and sensitivity of predicted native states to variations in the interaction schemes
- Statistical potentials for fold assessment
- Orientational potentials extracted from protein structures improve native fold recognition
- Database-derived potentials dependent on protein size for in silico folding and design.
- Conformation of polypeptides and proteins.
- Prediction of protein backbone conformation based on seven structure assignments. Influence of local interactions.
- Calculation of conformational ensembles from potentials of mean force. An approach to the knowledge-based prediction of local structures in globular proteins.
- Comparison of database potentials and molecular mechanics force fields.
- Knowledge-based potentials for proteins.
- PQS: a protein quaternary structure file server.
- Prediction of protein-folding mechanisms from free-energy landscapes derived from native structures.
- A lattice model for protein structure prediction at low resolution.
- Hydrophobicity of amino acid residues in globular proteins.
- Knowledge-based potential functions in protein design.
- Influence of protein structure databases on the predictive power of statistical pair potentials
- Dictionary of protein secondary structure: Pattern recognition of hydrogen‐bonded and geometrical features
- Potential energy functions.
Cited by
- Extending the PRIME Model for Protein Aggregation to All Twenty Amino Acids
- Discrimination of near-native decoy structures using statistical potentials
- Optimisation de potentiels statistiques pour un modèle d'évolution soumis à des contraintes structurales. (Optimization of statistical potentials for Structurally constrained phylogenetic models)
- A Review of Physics-Based Coarse-Grained Potentials for the Simulations of Protein Structure and Dynamics
- Computational Protein Design with Ensembles, Flexibility and Mathematical Guarantees, and its Application to Drug Resistance Prediction, and Antibody Design
- Towards an accurate prediction of the thermal stability of homologous proteins
- OPUS‐Ca: A knowledge‐based potential function requiring only Cα positions
- Predicting the Impact of Missense Mutations on Protein–Protein Binding Affinity
- Stability Curve Prediction of Homologous Proteins Using Temperature-Dependent Statistical Potentials
- Protein Conformation Motion Modeling Using Sep-CMA-ES
- Statistical energy potential: reduced representation of Dehouck–Gilis–Rooman function by selecting against decoy datasets
- Modelling Thermal Stability Changes Upon Mutations in Proteins with Artificial Neural Networks
- Hydrophobic potential of mean force as a solvation function for protein structure prediction.
- Computational design of protein-ligand interfaces: potential in therapeutic development
- Structure-based mutant stability predictions on proteins of unknown structure.
- Statistical potential for assessment and prediction of protein structures
- Perspective: Coarse-grained models for biomolecular systems.
- Neural networks to predict protein stability changes upon mutation
- PoPMuSiC 2.1: a web server for the estimation of protein stability changes upon mutation and sequence optimality
- Protein Design Using Continuous Rotamers
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