A. Makarov
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Research Subjects
Research Interests
A. Makarov has a total of 9 co-authors. Here are the top co-authors by number of shared publications:
A. Schulga
Centre Bioengineering, Russian Academy of Sciences, Moscow
1 shared publicationB. Ranjbar
Engelhardt Institute of Molecular Biology Russian Academy of Sciences 117984 Moscow
1 shared publicationF. Kurbanov
Centre 'Bioengineering' Russian Academy of Sciences 117312 Moscow
1 shared publicationI. Protasevich
Engelhardt Institute of Molecular Biology Russian Academy of Sciences 117984 Moscow
1 shared publication- Konstantin M. Polyakov
Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Vavilova Str. 32, Moscow 119991, Russian Federation
1 shared publication M. Kirpichnikov
Centre 'Bioengineering' Russian Academy of Sciences 117312 Moscow
1 shared publication
Latest Publications
- Open Access
- 1 September 1998
- Published by Oxford University Press (OUP) in Protein Engineering, Design and Selection
- Vol. 11 (9) , 775-782
Comparative study of binase and barnase: experience in chimeric ribonucleases
Chimeric enzymes were constructed to elucidate the differences in physicochemical properties of two related bacterial RNases, barnase and binase. Chimeras (Ba26Bi, Ba73Bi, Ba26Bi73Ba and Bi73Ba) contain six to thirteen residue substitutions relative to barnase, which are beyond the active site. The catalytic activity of RNases toward GpU, GpC and poly(I), as well as conformational distinctions and heat denaturation parameters, were studied. Thermal denaturation of binase, barnase and chimeric RNases is a two-state transition. The mutation-induced changes in the free energy of unfolding of barnase deduced from thermal and urea denaturation nearly coincide. The kinetic parameters for GpU and GpC demonstrate that the chimeras fall into two groups: barnase-like and binase-like. This division is determined by the origin of their C-terminal part (residues 73-110) which is also responsible for their thermostability at pH 2.4. An inverse linear dependence was found between kcat for poly(I) and denaturation temperature of RNases at pH 5.5, which points out that certain lability of the protein molecule appears to be necessary for efficient polynucleotide cleavage.
- 1 September 1998
- Published by Oxford University Press (OUP) in Protein Engineering, Design and Selection
- Vol. 11 (9) , 775-782
Open AccessComparative study of binase and barnase: experience in chimeric ribonucleases
Chimeric enzymes were constructed to elucidate the differences in physicochemical properties of two related bacterial RNases, barnase and binase. Chimeras (Ba26Bi, Ba73Bi, Ba26Bi73Ba and Bi73Ba) contain six to thirteen residue substitutions relative to barnase, which are beyond the active site. The catalytic activity of RNases toward GpU, GpC and poly(I), as well as conformational distinctions and heat denaturation parameters, were studied. Thermal denaturation of binase, barnase and chimeric RNases is a two-state transition. The mutation-induced changes in the free energy of unfolding of barnase deduced from thermal and urea denaturation nearly coincide. The kinetic parameters for GpU and GpC demonstrate that the chimeras fall into two groups: barnase-like and binase-like. This division is determined by the origin of their C-terminal part (residues 73-110) which is also responsible for their thermostability at pH 2.4. An inverse linear dependence was found between kcat for poly(I) and denaturation temperature of RNases at pH 5.5, which points out that certain lability of the protein molecule appears to be necessary for efficient polynucleotide cleavage.