| scholarly article | Q13442814 |
| P819 | ADS bibcode | 2000PNAS...97.3977B |
| P356 | DOI | 10.1073/PNAS.97.8.3977 |
| P932 | PMC publication ID | 18127 |
| P698 | PubMed publication ID | 10760269 |
| P5875 | ResearchGate publication ID | 12556689 |
| P2093 | author name string | Vendruscolo M | |
| Knapp EW | |||
| Bastolla U | |||
| P2860 | cites work | Protein Folding in Contact Map Space | Q21698714 |
| Errors in protein structures | Q27860776 | ||
| Principles that govern the folding of protein chains | Q28236872 | ||
| A Method to Identify Protein Sequences That Fold into a Known Three-Dimensional Structure | Q28282741 | ||
| Pathways to a protein folding intermediate observed in a 1-microsecond simulation in aqueous solution | Q28286232 | ||
| From Levinthal to pathways to funnels | Q28300934 | ||
| How to derive a protein folding potential? A new approach to an old problem | Q30426274 | ||
| Recovery of protein structure from contact maps | Q30428899 | ||
| Self-consistently optimized energy functions for protein structure prediction by molecular dynamics | Q30429818 | ||
| Designing potential energy functions for protein folding | Q33632621 | ||
| Spin glasses and the statistical mechanics of protein folding | Q34358450 | ||
| On the thermodynamic hypothesis of protein folding | Q36091068 | ||
| Enlarged representative set of protein structures | Q36278475 | ||
| Pair potentials for protein folding: choice of reference states and sensitivity of predicted native states to variations in the interaction schemes | Q36281424 | ||
| Derivation and testing of pair potentials for protein folding. When is the quasichemical approximation correct? | Q36850366 | ||
| Optimal protein-folding codes from spin-glass theory | Q37035526 | ||
| Protein tertiary structure recognition using optimized Hamiltonians with local interactions | Q37219203 | ||
| An iterative method for extracting energy-like quantities from protein structures. | Q37262313 | ||
| How optimization of potential functions affects protein folding | Q37611237 | ||
| On the theory of folding kinetics for short proteins. | Q46019059 | ||
| Testing a new Monte Carlo algorithm for protein folding | Q47810344 | ||
| Simulations of the folding of a globular protein | Q47890039 | ||
| Can a pairwise contact potential stabilize native protein folds against decoys obtained by threading? | Q52082394 | ||
| Protein folding mechanisms and the multidimensional folding funnel. | Q52237311 | ||
| Contact potential that recognizes the correct folding of globular proteins | Q52412013 | ||
| Calculation of conformational ensembles from potentials of mean force. An approach to the knowledge-based prediction of local structures in globular proteins. | Q52451138 | ||
| "New view" of protein folding reconciled with the old through multiple unfolding simulations. | Q52528318 | ||
| Master Equation Approach to Protein Folding and Kinetic Traps | Q58495842 | ||
| Identification of native protein folds amongst a large number of incorrect models. The calculation of low energy conformations from potentials of mean force | Q68363646 | ||
| Universality and diversity of the protein folding scenarios: a comprehensive analysis with the aid of a lattice model | Q73174194 | ||
| Factors that affect the folding ability of proteins | Q74631425 | ||
| Protein dynamics with off-lattice Monte Carlo moves | Q78077224 | ||
| P433 | issue | 8 | |
| P407 | language of work or name | English | Q1860 |
| P921 | main subject | statistics | Q12483 |
| protein folding | Q847556 | ||
| P304 | page(s) | 3977-3981 | |
| P577 | publication date | 2000-04-01 | |
| P1433 | published in | Proceedings of the National Academy of Sciences of the United States of America | Q1146531 |
| P1476 | title | A statistical mechanical method to optimize energy functions for protein folding | |
| P478 | volume | 97 |
| Q47304975 | A new parameter-rich structure-aware mechanistic model for amino acid substitution during evolution. |
| Q42708071 | Assessment of the quality of energy functions for protein folding by using a criterion derived with the help of the noisy go model |
| Q28241164 | Comparison of the transition state ensembles for folding of Im7 and Im9 determined using all-atom molecular dynamics simulations with phi value restraints |
| Q38223691 | Detecting selection on protein stability through statistical mechanical models of folding and evolution |
| Q30420867 | Distance dependency and minimum amino acid alphabets for decoy scoring potentials |
| Q57953582 | Folding of a small helical protein using hydrogen bonds and hydrophobicity forces |
| Q31922968 | How to guarantee optimal stability for most representative structures in the Protein Data Bank. |
| Q57483275 | Influence of mutation bias and hydrophobicity on the substitution rates and sequence entropies of protein evolution |
| Q57218694 | Lack of self-averaging in neutral evolution of proteins |
| Q33692707 | Molecular and Functional Bases of Selection against a Mutation Bias in an RNA Virus. |
| Q35222696 | On simplified global nonlinear function for fitness landscape: a case study of inverse protein folding |
| Q30371877 | Optimized distance-dependent atom-pair-based potential DOOP for protein structure prediction. |
| Q30400418 | Protein side chain modeling with orientation-dependent atomic force fields derived by series expansions |
| Q52076418 | Recurrent oligomers in proteins: an optimal scheme reconciling accurate and concise backbone representations in automated folding and design studies. |
| Q22066374 | Reductive genome evolution in Buchnera aphidicola |
| Q47720602 | Sequence determinants of protein folding rates: positive correlation between contact energy and contact range indicates selection for fast folding |
| Q30404525 | Statistical mechanics-based method to extract atomic distance-dependent potentials from protein structures |
| Q29615145 | Statistical potential for assessment and prediction of protein structures |
| Q35635713 | Statistical potential for modeling and ranking of protein-ligand interactions |
| Q30385705 | Statistical potentials for improved structurally constrained evolutionary models. |
| Q47982690 | Statistical properties of neutral evolution |
| Q47222730 | Substitution rates predicted by stability-constrained models of protein evolution are not consistent with empirical data |
| Q21686181 | Teaching computers to fold proteins |
| Q37037782 | Why should we care about molecular coevolution? |
| Q42023667 | toyLIFE: a computational framework to study the multi-level organisation of the genotype-phenotype map. |
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