{"doi":"10.1039/c1mb05367a","title":"Meta-structure correlation in protein space unveils different selection rules for folded and intrinsically disordered proteins","abstract":"<jats:title>Abstract</jats:title>\n                  <jats:p>The number of existing protein sequences spans a very small fraction of sequence space. Natural proteins have overcome a strong negative selective pressure to avoid the formation of insoluble aggregates. Stably folded globular proteins and intrinsically disordered proteins (IDPs) use alternative solutions to the aggregation problem. While in globular proteins folding minimizes the access to aggregation prone regions, IDPs on average display large exposed contact areas. Here, we introduce the concept of average meta-structure correlation maps to analyze sequence space. Using this novel conceptual view we show that representative ensembles of folded and IDproteins show distinct characteristics and respond differently to sequence randomization. By studying the way evolutionary constraints act on IDPs to disable a negative function (aggregation) we might gain insight into the mechanisms by which function-enabling information is encoded in IDPs.</jats:p>\n                  <jats:p/>","journal":"Molecular BioSystems","year":2011,"id":682714,"datarank":0.40620753016533157,"base_score":2.70805020110221,"endowment":2.70805020110221,"self_citation_contribution":0.40620753016533157,"citation_network_contribution":0.0,"self_endowment_contribution":0.40620753016533157,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":14,"citer_count":0,"citers_with_citation_signal":0,"citers_with_endowment":0,"datacite_reuse_total":0,"is_dataset":false,"is_dataset_confidence":null,"is_data_producer":false,"deposit_databanks":null,"is_oa":false,"file_count":0,"downloads":0,"has_version_chain":false,"published_date":null,"fair_score":null,"fair_percentile":null,"algorithm_id":"datarank_citation_only_1hop_v6","ranking_scope":"data_only","authors":[{"id":996447,"name":"Miquel Pons","orcid":"0000-0002-0586-8322","position":1,"is_corresponding":false},{"id":1163659,"name":"Robert Konrat","orcid":"0000-0001-6489-4080","position":2,"is_corresponding":false},{"id":1783521,"name":"Yandi Naranjo","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"Meta-structure correlation in protein space unveils different selection rules for folded and intrinsically disordered proteins","abstract":"<jats:title>Abstract</jats:title>\n                  <jats:p>The number of existing protein sequences spans a very small fraction of sequence space. Natural proteins have overcome a strong negative selective pressure to avoid the formation of insoluble aggregates. Stably folded globular proteins and intrinsically disordered proteins (IDPs) use alternative solutions to the aggregation problem. While in globular proteins folding minimizes the access to aggregation prone regions, IDPs on average display large exposed contact areas. Here, we introduce the concept of average meta-structure correlation maps to analyze sequence space. Using this novel conceptual view we show that representative ensembles of folded and IDproteins show distinct characteristics and respond differently to sequence randomization. By studying the way evolutionary constraints act on IDPs to disable a negative function (aggregation) we might gain insight into the mechanisms by which function-enabling information is encoded in IDPs.</jats:p>\n                  <jats:p/>","is_dataset_classified":null,"base_score":2.70805020110221,"endowment":2.70805020110221,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"22108787","pmcid":null,"openalex_id":"https://openalex.org/W2046702940","authors":[],"funders":[{"funder_name":"European Commission","grant_id":"261863","title":"NMR for Structural Biology"}],"total_grants":1,"fwci":0.6084,"citation_percentile":0.65697478,"influential_citations":0,"citation_trend":[{"year":2013,"count":3},{"year":2014,"count":2},{"year":2015,"count":1},{"year":2017,"count":1},{"year":2018,"count":1},{"year":2019,"count":5},{"year":2022,"count":1}],"oa_status":"closed","license":"OUP Standard Publication Reuse","oa_locations":[{"url":"https://academic.oup.com/molecular-omics/article-pdf/8/1/411/66158031/c1mb05367a.pdf","host_type":"publisher"},{"url":"https://doi.org/10.1039/c1mb05367a","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/22108787","host_type":"repository"},{"url":"https://hdl.handle.net/2445/47843","host_type":"repository"},{"url":"http://hdl.handle.net/2445/47843","host_type":"repository"},{"url":"http://diposit.ub.edu/dspace/bitstream/2445/47843/1/607143.pdf","host_type":""},{"url":"https://dx.doi.org/10.1039/c1mb05367a","host_type":""},{"url":"http://dx.doi.org/10.1039/c1mb05367a","host_type":""}],"fields_of_study":["Protein Structure and Dynamics","Enzyme Structure and Function","Proteins in Food Systems","0301 basic medicine","0303 health sciences","03 medical and health sciences","Algorithms","Amino Acid Sequence","Amino Acids","Amyloid","Cluster Analysis","Databases, Protein","Protein Conformation","Protein Folding","Proteins"],"mesh_terms":["Algorithms","Amino Acid Sequence","Amino Acids","Amyloid","Protein Conformation","Proteins","Cluster Analysis","Protein Folding","Databases, Protein"],"keywords":["Sequence space","Intrinsically disordered proteins","Globular protein","Sequence (biology)","Folding (DSP implementation)","Protein folding","Function (biology)","Computational biology","Space (punctuation)","Computer science","Biological system","Biology","Biophysics","Mathematics","Evolutionary biology","Genetics","Biochemistry","Biomolecules","Amyloid","Bioinformatics","Protein Conformation","Àcids nucleics","Proteins","Ressonància magnètica nuclear","Nuclear magnetic resonance","Amino acid sequence","Nucleic acids","Biomolècules","Bioinformàtica","Seqüència d'aminoàcids","Cluster Analysis","Amino Acids","Databases, Protein","Algorithms"],"sdg_mappings":[],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-08-17T21:10:54.216742Z","pmid":null,"pmcid":null,"fwci":null,"citation_percentile":null,"influential_citations":0,"oa_status":null,"license":null,"views":0,"total_file_size_bytes":0,"version_count":0,"fair_f":null,"fair_a":null,"fair_i":null,"fair_r":null,"fair_zscore":null,"fair_rationale":null,"fair_model":null,"fair_agent_version":null,"fair_fulltext_source":null,"fair_has_llm":null,"fair_computed_at":null,"clinical_trials":[],"software_tools":[],"db_accessions":[],"linked_datasets":[],"topics":[]}