Oleg B. Ptitsyn

Affiliations: 
Laboratory of Protein Physics Institute of Protein Research, Russian Academy of Sciences 
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"Oleg Ptitsyn"
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Tcherkasskaya O, Ptitsyn OB, Knutson JR. (2000) Nanosecond dynamics of tryptophans in different conformational states of apomyoglobin proteins. Biochemistry. 39: 1879-89
Ptitsyn OB, Ting KL. (1999) Non-functional conserved residues in globins and their possible role as a folding nucleus. Journal of Molecular Biology. 291: 671-82
Tcherkasskaya O, Ptitsyn OB. (1999) Molten globule versus variety of intermediates: influence of anions on pH-denatured apomyoglobin. Febs Letters. 455: 325-31
Tcherkasskaya O, Ptitsyn OB. (1999) Direct energy transfer to study the 3D structure of non-native proteins: AGH complex in molten globule state of apomyoglobin. Protein Engineering. 12: 485-90
Ptitsyn OB. (1999) Protein evolution and protein folding: non-functional conserved residues and their probable role. Pacific Symposium On Biocomputing. Pacific Symposium On Biocomputing. 494-504
Bychkova VE, Dujsekina AE, Fantuzzi A, et al. (1998) Release of retinol and denaturation of its plasma carrier, retinol-binding protein. Folding & Design. 3: 285-91
Afasizheva IIu, Dolgikh DA, Abdullaev ZKh, et al. (1998) [Effect of a biologically active interferon fragment on the structure of the synthetic protein carrier]. Biofizika. 43: 384-91
Ptitsyn OB. (1998) Protein folding and protein evolution: common folding nucleus in different subfamilies of c-type cytochromes? Journal of Molecular Biology. 278: 655-66
Ptitsyn OB. (1998) Protein folding: nucleation and compact intermediates. Biochemistry. Biokhimiia. 63: 367-73
Aphasizheva IY, Dolgikh DA, Abdullaev ZK, et al. (1998) Can grafting of an octapeptide improve the structure of a de novo protein? Febs Letters. 425: 101-4
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