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FEBS Letters|August 7, 1999
Molten globule versus variety of intermediates: influence of anions on pH-denatured apomyoglobinO Tcherkasskaya, O B PtitsynMolecular Biology|January 1, 1975
The structure of hydrophobic cores of globinsS A Kozitsyn, O B PtitsynTsitologiia|January 1, 1995
[The functional state of denatured proteins: the principles of modelling and the first results]V E Bychkova, O B PtitsynProtein Engineering|August 1, 1989
Binding of the globular domain of linker histones H5/H1 to the nucleosome: a hypothesisC Crane-Robinson, O B PtitsynFEBS Letters|November 2, 1987
An early intermediate of refolding alpha-lactalbumin forms within 20 msR I Gilmanshin, O B PtitsynMolekuliarnaia Biologiia|July 1, 1976
Thermodynamic parameters of helix-random coil transitions in polypeptide chains. IV. Random copolymers of L-alanine with L-glutamic acidV E Bychkova, O B PtitsynProtein Engineering|March 1, 1989
Prediction of protein secondary structure based on physical theory. HistonesO B Ptitsyn, A V FinkelsteinJournal of Molecular Biology|August 17, 1999
Non-functional conserved residues in globins and their possible role as a folding nucleusO B Ptitsyn, K L TingFEBS Letters|February 6, 1995
Folding intermediates are involved in genetic diseases?V E Bychkova, O B PtitsynBiofizika|January 1, 1993
[The state of unfolded globules of protein molecules is more quickly becoming a rule, rather than an exception]V E Bychkova, O B PtitsynPageof 7