| scholarly article | Q13442814 |
| P50 | author | Valerie Daggett | Q7911257 |
| R. Dustin Schaeffer | Q42847625 | ||
| P2860 | cites work | Design of a Novel Globular Protein Fold with Atomic-Level Accuracy | Q22242282 |
| A fully automatic evolutionary classification of protein folds: Dali Domain Dictionary version 3 | Q24605760 | ||
| A consensus view of fold space: Combining SCOP, CATH, and the Dali Domain Dictionary | Q24647013 | ||
| The Pfam protein families database | Q24650035 | ||
| The structural alignment between two proteins: is there a unique answer? | Q24673989 | ||
| CDD: a conserved domain database for interactive domain family analysis | Q24675724 | ||
| Structural analysis of WW domains and design of a WW prototype | Q27622470 | ||
| The helix turn helix motif as an ultrafast independently folding domain: The pathway of folding of Engrailed homeodomain | Q27644846 | ||
| Touring protein fold space with Dali/FSSP | Q27860559 | ||
| SCOP: a structural classification of proteins database for the investigation of sequences and structures | Q27860689 | ||
| CATH--a hierarchic classification of protein domain structures | Q27861100 | ||
| Mapping the protein universe | Q27861112 | ||
| A systematic comparison of protein structure classifications: SCOP, CATH and FSSP | Q28145483 | ||
| Protein superfamilies and domain superfolds | Q28242652 | ||
| Structural patterns in globular proteins | Q28252376 | ||
| One thousand families for the molecular biologist | Q28266140 | ||
| Identification and analysis of domains in proteins | Q28271429 | ||
| Data growth and its impact on the SCOP database: new developments | Q29619285 | ||
| Partitioning protein structures into domains: why is it so difficult? | Q29994424 | ||
| Toward consistent assignment of structural domains in proteins | Q29994428 | ||
| Identification of homology in protein structure classification. | Q30329161 | ||
| Protein structure comparison: implications for the nature of 'fold space', and structure and function prediction. | Q30354243 | ||
| Growth of novel protein structural data. | Q30360459 | ||
| Cradle-loop barrels and the concept of metafolds in protein classification by natural descent. | Q30369261 | ||
| Cross-over between discrete and continuous protein structure space: insights into automatic classification and networks of protein structures. | Q30375822 | ||
| Systematic comparison of SCOP and CATH: a new gold standard for protein structure analysis. | Q30376232 | ||
| Nothing about protein structure classification makes sense except in the light of evolution. | Q30376508 | ||
| Discrete-continuous duality of protein structure space. | Q30377688 | ||
| SSAP: sequential structure alignment program for protein structure comparison | Q30424679 | ||
| Dictionary of recurrent domains in protein structures | Q30431465 | ||
| Estimating the number of protein folds and families from complete genome data | Q30597194 | ||
| Ensemble versus single-molecule protein unfolding | Q31004121 | ||
| The complete folding pathway of a protein from nanoseconds to microseconds | Q33186113 | ||
| Refolding the Engrailed Homeodomain: Structural Basis for the Accumulation of a Folding Intermediate | Q33349725 | ||
| Estimating the total number of protein folds | Q33866133 | ||
| A comprehensive multidimensional-embedded, one-dimensional reaction coordinate for protein unfolding/folding | Q33880409 | ||
| Dynameomics: a comprehensive database of protein dynamics | Q33943177 | ||
| Microscopic reversibility of protein folding in molecular dynamics simulations of the engrailed homeodomain | Q34001026 | ||
| Keeping it in the family: folding studies of related proteins | Q34141529 | ||
| Fold change in evolution of protein structures | Q34364834 | ||
| The CATH domain structure database: new protocols and classification levels give a more comprehensive resource for exploring evolution | Q34585750 | ||
| Is there a unifying mechanism for protein folding? | Q35040955 | ||
| Protein folding from a highly disordered denatured state: the folding pathway of chymotrypsin inhibitor 2 at atomic resolution | Q35246273 | ||
| Protein folding and unfolding in microseconds to nanoseconds by experiment and simulation | Q35566520 | ||
| Direct observation of microscopic reversibility in single-molecule protein folding | Q35830095 | ||
| Structure of the transition state for the folding/unfolding of the barley chymotrypsin inhibitor 2 and its implications for mechanisms of protein folding. | Q35854484 | ||
| Characterization of the transition state of protein unfolding by use of molecular dynamics: chymotrypsin inhibitor 2 | Q35855081 | ||
| The family feud: do proteins with similar structures fold via the same pathway? | Q36046430 | ||
| Synergy between simulation and experiment in describing the energy landscape of protein folding | Q36199011 | ||
| Molecular dynamics simulation of cytochrome b5: implications for protein-protein recognition | Q36688856 | ||
| Dynameomics: large-scale assessment of native protein flexibility | Q36990639 | ||
| Unifying features in protein-folding mechanisms | Q37088491 | ||
| Dynameomics: a consensus view of the protein unfolding/folding transition state ensemble across a diverse set of protein folds | Q37443818 | ||
| Advances and pitfalls of protein structural alignment | Q37501173 | ||
| Fold space unlimited | Q37509602 | ||
| What lessons can be learned from studying the folding of homologous proteins? | Q37767065 | ||
| Jamming of soft particles: geometry, mechanics, scaling and isostaticity | Q37850912 | ||
| A rapid classification protocol for the CATH Domain Database to support structural genomics | Q38661201 | ||
| Protein folds and families: sequence and structure alignments | Q39726503 | ||
| Gene3D: structural assignment for whole genes and genomes using the CATH domain structure database | Q39753565 | ||
| Population statistics of protein structures: lessons from structural classifications | Q41515810 | ||
| The CATH hierarchy revisited-structural divergence in domain superfamilies and the continuity of fold space | Q42551770 | ||
| Biological meaning, statistical significance, and classification of local spatial similarities in nonhomologous proteins | Q42844240 | ||
| The CATH classification revisited--architectures reviewed and new ways to characterize structural divergence in superfamilies | Q42875582 | ||
| The role of the turn in beta-hairpin formation during WW domain folding | Q42959556 | ||
| Dynameomics: mass annotation of protein dynamics and unfolding in water by high-throughput atomistic molecular dynamics simulations | Q44637148 | ||
| NMR studies of the association of cytochrome b5 with cytochrome c. | Q46369525 | ||
| Simulation and experiment conspire to reveal cryptic intermediates and a slide from the nucleation-condensation to framework mechanism of folding | Q46557310 | ||
| Phi-analysis at the experimental limits: mechanism of beta-hairpin formation | Q47602407 | ||
| Structural diversity of domain superfamilies in the CATH database | Q47602442 | ||
| Diffusing and colliding: the atomic level folding/unfolding pathway of a small helical protein | Q47609351 | ||
| Engineering out motion: a surface disulfide bond alters the mobility of tryptophan 22 in cytochrome b5 as probed by time-resolved fluorescence and 1H NMR experiments | Q47623554 | ||
| Engineering out motion: introduction of a de novo disulfide bond and a salt bridge designed to close a dynamic cleft on the surface of cytochrome b5. | Q47623569 | ||
| Structure of the transition state for folding of a protein derived from experiment and simulation | Q47629796 | ||
| Identification and characterization of the unfolding transition state of chymotrypsin inhibitor 2 by molecular dynamics simulations | Q47629807 | ||
| Solution structure of a protein denatured state and folding intermediate. | Q51339720 | ||
| Estimating the number of protein folds. | Q52907614 | ||
| Relations of the numbers of protein sequences, families and folds. | Q54562558 | ||
| A unifold, mesofold, and superfold model of protein fold use | Q57972079 | ||
| How many fold types of protein are there in nature? | Q71774362 | ||
| Understanding protein flexibility through dimensionality reduction | Q73845550 | ||
| P433 | issue | 1-2 | |
| P921 | main subject | protein folding | Q847556 |
| P304 | page(s) | 11-19 | |
| P577 | publication date | 2010-11-03 | |
| P1433 | published in | Protein Engineering Design and Selection | Q15762396 |
| P1476 | title | Protein folds and protein folding | |
| P478 | volume | 24 |
| Q38387036 | A survey of transposable element classification systems--a call for a fundamental update to meet the challenge of their diversity and complexity. |
| Q47667810 | Accelerating physical simulations of proteins by leveraging external knowledge. |
| Q27679488 | Conservation of Protein Structure over Four Billion Years |
| Q104474717 | De Novo Protein Design Using the Blueprint Builder in Rosetta |
| Q47583342 | Dynameomics: protein dynamics and unfolding across fold space |
| Q41904524 | Energetic frustrations in protein folding at residue resolution: a homologous simulation study of Im9 proteins. |
| Q59051409 | Exact Solution to the Extended Zwanzig Model for Quasi-Sigmoidal Chemically Induced Denaturation Profiles: Specific Heat and Configurational Entropy |
| Q30396098 | Generation of a consensus protein domain dictionary |
| Q35838944 | Independent structural domains in paramyxovirus polymerase protein |
| Q57329073 | Modeling Protein Folding Pathways |
| Q31035956 | New Dynamic Rotamer Libraries: Data-Driven Analysis of Side-Chain Conformational Propensities |
| Q46082224 | On the universe of protein folds |
| Q27696008 | Prioritizing targets for structural biology through the lens of proteomics: the archaeal protein TGAM_1934 from Thermococcus gammatolerans |
| Q50725541 | Role of single-point mutations and deletions on transition temperatures in ideal proteinogenic heteropolymer chains in the gas phase. |
| Q60923976 | The Role of Hydrogen Bonding in the Folding/Unfolding Process of Hydrated Lysozyme: A Review of Recent NMR and FTIR Results |
| Q41783652 | When a domain is not a domain, and why it is important to properly filter proteins in databases: conflicting definitions and fold classification systems for structural domains make filtering of such databases imperative |
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