| scholarly article | Q13442814 |
| review article | Q7318358 |
| P356 | DOI | 10.1016/S0959-440X(97)80054-1 |
| P698 | PubMed publication ID | 9204279 |
| P50 | author | Cyrus Chothia | Q5201079 |
| Steven E. Brenner | Q7614656 | ||
| Tim Hubbard | Q15990056 | ||
| P2860 | cites work | Dali/FSSP classification of three-dimensional protein folds | Q24544111 |
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| Similarity of the three-dimensional structures of actin and the ATPase fragment of a 70-kDa heat shock cognate protein | Q37529426 | ||
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| Depicting topology and handedness in jellyroll structures | Q47636894 | ||
| The α-helix as seen from the protein tertiary structure: a 3-D structural classification | Q52340261 | ||
| Emergence of Preferred Structures in a Simple Model of Protein Folding | Q56517454 | ||
| How far can sequences diverge? | Q59072657 | ||
| Quantitative organization of the known protein x-ray structures. I. Methods and short-length-scale results | Q68878435 | ||
| A dynamic look at structures: WWW-Entrez and the Molecular Modeling Database | Q71356165 | ||
| Recognition of super-secondary structure in proteins | Q95807876 | ||
| P433 | issue | 3 | |
| P407 | language of work or name | English | Q1860 |
| P921 | main subject | statistics | Q12483 |
| P304 | page(s) | 369-376 | |
| P577 | publication date | 1997-06-01 | |
| P1433 | published in | Current Opinion in Structural Biology | Q15758416 |
| P1476 | title | Population statistics of protein structures: lessons from structural classifications | |
| P478 | volume | 7 |
| Q43849874 | A comparison of the urea-induced unfolding of apoflavodoxin and flavodoxin from Desulfovibrio vulgaris |
| Q24548236 | A database of macromolecular motions |
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| Q42847317 | Apoflavodoxin (un)folding followed at the residue level by NMR. |
| Q37379451 | Assessing sequence comparison methods with reliable structurally identified distant evolutionary relationships |
| Q48566951 | CAMPASS: a database of structurally aligned protein superfamilies |
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| Q30375822 | Cross-over between discrete and continuous protein structure space: insights into automatic classification and networks of protein structures. |
| Q30331544 | Designability of alpha-helical proteins |
| Q42732257 | Diversity of functions of proteins with internal symmetry in spatial arrangement of secondary structural elements |
| Q77326443 | Errors in genome annotation |
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| Q30353443 | Exploring dynamics of protein structure determination and homology-based prediction to estimate the number of superfamilies and folds. |
| Q48105871 | From sequences to a functional unit |
| Q34635987 | Frustration in biomolecules |
| Q24814930 | Functional coverage of the human genome by existing structures, structural genomics targets, and homology models |
| Q30336447 | Functional prediction of a T-DNA tagged gene of Arabidopsis thaliana by in silico analysis. |
| Q48168102 | Gene conversion and functional divergence in the beta-globin gene family |
| Q30360459 | Growth of novel protein structural data. |
| Q52956083 | How Well is Enzyme Function Conserved as a Function of Pairwise Sequence Identity? |
| Q31934081 | How representative are the known structures of the proteins in a complete genome? A comprehensive structural census |
| Q52411803 | Identification of protein functions from a molecular surface database, eF-site. |
| Q41816440 | Identification of the ligand binding sites on the molecular surface of proteins |
| Q77926218 | Identifying proteins of high designability via surface-exposure patterns |
| Q34368001 | Issues in bioinformatics benchmarking: the case study of multiple sequence alignment |
| Q43032817 | MALISAM: a database of structurally analogous motifs in proteins |
| Q33948562 | Mapping the folding pathway of an immunoglobulin domain: structural detail from Phi value analysis and movement of the transition state |
| Q42846626 | Mechanics and dynamics of B1 domain of protein G: role of packing and surface hydrophobic residues |
| Q30327431 | Methodologies for target selection in structural genomics. |
| Q31035956 | New Dynamic Rotamer Libraries: Data-Driven Analysis of Side-Chain Conformational Propensities |
| Q57822025 | No cofactor effect on equilibrium unfolding of Desulfovibrio desulfuricans flavodoxin |
| Q46082224 | On the universe of protein folds |
| Q30329284 | PASS2: a semi-automated database of protein alignments organised as structural superfamilies. |
| Q30432219 | Patterns of protein-fold usage in eight microbial genomes: a comprehensive structural census |
| Q38072997 | Polyproline and triple helix motifs in host-pathogen recognition |
| Q51082531 | Precursory signatures of protein folding/unfolding: from time series correlation analysis to atomistic mechanisms. |
| Q33950359 | Protein folding and stability investigated by fluorescence, circular dichroism (CD), and nuclear magnetic resonance (NMR) spectroscopy: the flavodoxin story |
| Q34412995 | Protein folds and protein folding |
| Q35014296 | Protein modules and protein-protein interaction. Introduction |
| Q30329464 | Protein topology and stability define the space of allowed sequences. |
| Q42432017 | QSCOP-BLAST--fast retrieval of quantified structural information for protein sequences of unknown structure |
| Q47615016 | Quantifying the similarities within fold space |
| Q73259559 | Quo vadis, biotech? (Part 1) |
| Q35070215 | Relative packing groups in template-based structure prediction: cooperative effects of true positive constraints |
| Q52229910 | SCOP: a Structural Classification of Proteins database. |
| Q45961452 | Shining a light on structural genomics. |
| Q57830269 | Stabilisation centres differ between structurally homologous proteins as shown by NMR spectroscopy |
| Q46486615 | Structural and functional characterization of AtPTR3, a stress-induced peptide transporter of Arabidopsis. |
| Q27638461 | Structural genomics: A pipeline for providing structures for the biologist |
| Q33744732 | Structural genomics: beyond the human genome project |
| Q59063653 | Structure space of model proteins: A principal component analysis |
| Q52950780 | Sustained Microtubule Treadmilling in Arabidopsis Cortical Arrays |
| Q28139937 | The ASTRAL compendium for protein structure and sequence analysis |
| Q47621170 | The CATH Dictionary of Homologous Superfamilies (DHS): a consensus approach for identifying distant structural homologues |
| Q90623761 | The Urfold: Structural similarity just above the superfold level? |
| Q30327381 | The current excitement in bioinformatics-analysis of whole-genome expression data: how does it relate to protein structure and function? |
| Q77476305 | The cystine knot structure of ion channel toxins and related polypeptides |
| Q73944439 | The designability of protein structures |
| Q42174587 | The equilibrium unfolding of Azotobacter vinelandii apoflavodoxin II occurs via a relatively stable folding intermediate |
| Q34613438 | The evolutionary analysis of "orphans" from the Drosophila genome identifies rapidly diverging and incorrectly annotated genes |
| Q34636738 | The impact of extremophiles on structural genomics (and vice versa). |
| Q30326945 | The role of protein structure in genomics. |
| Q38270675 | Thoroughly sampling sequence space: large-scale protein design of structural ensembles |
| Q41821911 | Tryptophan-tryptophan energy migration as a tool to follow apoflavodoxin folding |
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