CORD-19:f212d6366a45726107a30bde1f4615c28cb5ce22 / 37637-38028
Annnotations
{"target":"https://pubannotation.org/docs/sourcedb/CORD-19/sourceid/f212d6366a45726107a30bde1f4615c28cb5ce22","sourcedb":"CORD-19","sourceid":"f212d6366a45726107a30bde1f4615c28cb5ce22","text":"In general, the conformational behavior of IDPs is characterized by the low cooperativity (or the complete lack thereof) of the denaturant-induced unfolding, lack of the measurable excess heat absorption peak(s) characteristic for the melting of ordered proteins, \"turned out\" response to heat and changes in pH, and the ability to gain structure in the presence of various binding partners.","tracks":[{"project":"CORD-19_Custom_license_subset","denotations":[{"id":"T179","span":{"begin":0,"end":391},"obj":"Sentence"}],"attributes":[{"subj":"T179","pred":"source","obj":"CORD-19_Custom_license_subset"}]},{"project":"CORD-19-Sentences","denotations":[{"id":"TextSentencer_T179","span":{"begin":0,"end":391},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"attributes":[{"subj":"TextSentencer_T179","pred":"source","obj":"CORD-19-Sentences"}]}],"config":{"attribute types":[{"pred":"source","value type":"selection","values":[{"id":"CORD-19_Custom_license_subset","color":"#ec93dd","default":true},{"id":"CORD-19-Sentences","color":"#93ece0"}]}]}}