Cold Denaturation and Aggregation: A Comparative NMR Study of Titin I28 in Bulk and in a Confined Environment

scientific article published on 01 August 2009

Cold Denaturation and Aggregation: A Comparative NMR Study of Titin I28 in Bulk and in a Confined Environment is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1021/JA904462N
P698PubMed publication ID19653628

P50authorAnnalisa PastoreQ21254211
Domenico SanfeliceQ50422006
Anastasia PolitouQ117275843
P2093author name stringPiero A Temussi
Teodorico Tancredi
P433issue33
P407language of work or nameEnglishQ1860
P304page(s)11662-11663
P577publication date2009-08-01
P1433published inJournal of the American Chemical SocietyQ898902
P1476titleCold denaturation and aggregation: a comparative NMR study of titin I28 in bulk and in a confined environment
P478volume131

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cites work (P2860)
Q35729373"Invisible" conformers of an antifungal disulfide protein revealed by constrained cold and heat unfolding, CEST-NMR experiments, and molecular dynamics calculations.
Q28088466Beyond the excluded volume effects: mechanistic complexity of the crowded milieu
Q36351593Cold denaturation as a tool to measure protein stability
Q57956349Cold unfolding of β-hairpins: A molecular-level rationalization
Q43607840Molecular dynamics simulation indicating cold denaturation of β-hairpins
Q30402232NMR-based structural biology of proteins in supercooled water
Q57956344On the effect of low concentrations of alcohols on the conformational stability of globular proteins
Q50885962Solvent effects in the helix-coil transition model can explain the unusual biophysics of intrinsically disordered proteins.
Q42557982The cold denatured state of the C-terminal domain of protein L9 is compact and contains both native and non-native structure

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