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Biophysical Chemistry|February 1, 1975
A model of myoglobin self-organizationO B Ptitsyn, A A Rashin
Molekuliarnaia Biologiia|May 1, 1984
[Protein as an edited random copolymer]O B Ptitsyn
FEBS Letters|July 22, 1991
How does protein synthesis give rise to the 3D-structure?O B Ptitsyn
Current Opinion in Structural Biology|February 1, 1995
Structures of folding intermediatesO B Ptitsyn
Pacific Symposium on Biocomputing. Pacific Symposium on Biocomputing|June 25, 1999
Protein evolution and protein folding: non-functional conserved residues and their probable roleO B Ptitsyn
Biochemistry. Biokhimiia|April 29, 1998
Protein folding: nucleation and compact intermediatesO B Ptitsyn
Journal of Molecular Biology|June 20, 1998
Protein folding and protein evolution: common folding nucleus in different subfamilies of c-type cytochromes?O B Ptitsyn
Protein Engineering|July 2, 1999
Direct energy transfer to study the 3D structure of non-native proteins: AGH complex in molten globule state of apomyoglobinO Tcherkasskaya, O B Ptitsyn
FEBS Letters|August 7, 1999
Molten globule versus variety of intermediates: influence of anions on pH-denatured apomyoglobinO Tcherkasskaya, O B Ptitsyn
Molecular Biology|January 1, 1975
The structure of hydrophobic cores of globinsS A Kozitsyn, O B Ptitsyn
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