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Biophysical Chemistry|June 1, 2015
Cold denaturation as a tool to measure protein stabilityDomenico Sanfelice, Piero Andrea TemussiChemphyschem : a European Journal of Chemical Physics and Physical Chemistry|October 2, 2015
Cold Denaturation Unveiled: Molecular Mechanism of the Asymmetric Unfolding of Yeast FrataxinDomenico Sanfelice, Edoardo Morandi, Annalisa Pastore, et al.Nature Communications|May 19, 2017
An optimized strategy to measure protein stability highlights differences between cold and hot unfolded statesCaterina Alfano, Domenico Sanfelice, Stephen R Martin, et al.Protein Science : a Publication of the Protein Society|March 17, 2015
Selective observation of the disordered import signal of a globular protein by in-cell NMR: the example of frataxinsMatija Popovic, Domenico Sanfelice, Chiara Pastore, et al.Plos One|May 8, 2014
Yeast frataxin is stabilized by low salt concentrations: cold denaturation disentangles ionic strength effects from specific interactionsDomenico Sanfelice, Rita Puglisi, Stephen R Martin, et al.Journal of Molecular Recognition : JMR|November 1, 2011
Determinants of sweetness in proteins: a topological approachPiero Andrea TemussiTrends in Biochemical Sciences|May 16, 2009
Sweet, bitter and umami receptors: a complex relationshipPiero Andrea TemussiFEBS Letters|September 5, 2002
Why are sweet proteins sweet? Interaction of brazzein, monellin and thaumatin with the T1R2-T1R3 receptorPiero Andrea TemussiCurrent Opinion in Structural Biology|December 14, 2011
The two faces of Janus: functional interactions and protein aggregationAnnalisa Pastore, Piero Andrea TemussiChembiochem : a European Journal of Chemical Biology|May 8, 2023
Unfolding under Pressure: An NMR PerspectiveAnnalisa Pastore, Piero Andrea TemussiPageof 8