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B P Atanasov

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Molekuliarnaia Biologiia|January 1, 1979
[Studies of the pH-induced conformational changes in the N- and C-terminals of the spin-labelled sperm whale myoglobin molecule]R I Artiukh, B P Atanasov, M V Vol'kenshteĭn
Biopolymers|October 1, 1971
Thermodynamic analysis of thermal transitions in globular proteins. I. Calorimetric study of chymotrypsinogen, ribonuclease and myoglobinP L Privalov, N N Khechinashvili, B P Atanasov
Biochimica Et Biophysica Acta|June 15, 1976
Dependence of magneto-optical rotatory dispersion and magnetic circular dichroism of deoxy- and methemoglobin on their quaternary structureY A Sharonov, N A Sharonova, B P Atanasov
Molekuliarnaia Biologiia|March 1, 1977
[Conformation properties of sperm whale myoglobin modified by spin labels on histidyl residues]R I Artiukh, B P Atanasov, M V Vol'kenshteĭn
Biochimica Et Biophysica Acta|November 23, 1988
pH-dependence of photo-induced electron transfer in zinc-substituted sperm whale myoglobinA C Shosheva, P K Christova, B P Atanasov
Biochimica Et Biophysica Acta|July 27, 1970
Haem hydration and displacement in the pre-denaturational conformational transition of the myoglobin moleculeA Derzhanski, A Georgieva, K Kotev, et al.
Molecular Biology|January 1, 1972
Calorimetric investigations on heat denaturation of cyanmetmyoglobinB P Atanasov, P L Privalov, N N Khechinashvili
Molekuliarnaia Biologiia|January 1, 1982
[Electron transfer in hemoproteins. VIII. Influence of ionic strength on the rate of reduction of ferricytochrome c by oxymyoglobin derivatives, chemically modified at histidine residues]G B Postnikova, E A Shliapnikova, B P Atanasov, et al.
Molekuliarnaia Biologiia|May 1, 1975
[Selected carboxymethylation of ferri-hemoglobin from insect larvae Chironomus thummi thummi]R I Artoiukh, B P Atanasov, M V Vol'kenshteĭn, et al.
Molekuliarnaia Biologiia|May 1, 1981
[Electron transfer in hemoproteins. VI. The dependence of the reduction rate of ferricytochrome c by oxymyoglobin on ionic strength]G B Postnikova, E A Shliapnikova, M V Vol'kenshteĭn, et al.
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Showing results (11-20 of 31) with videos related to

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Molekuliarnaia Biologiia|January 1, 1979
[Studies of the pH-induced conformational changes in the N- and C-terminals of the spin-labelled sperm whale myoglobin molecule]R I Artiukh, B P Atanasov, M V Vol'kenshteĭn
Biopolymers|October 1, 1971
Thermodynamic analysis of thermal transitions in globular proteins. I. Calorimetric study of chymotrypsinogen, ribonuclease and myoglobinP L Privalov, N N Khechinashvili, B P Atanasov
Biochimica Et Biophysica Acta|June 15, 1976
Dependence of magneto-optical rotatory dispersion and magnetic circular dichroism of deoxy- and methemoglobin on their quaternary structureY A Sharonov, N A Sharonova, B P Atanasov
Molekuliarnaia Biologiia|March 1, 1977
[Conformation properties of sperm whale myoglobin modified by spin labels on histidyl residues]R I Artiukh, B P Atanasov, M V Vol'kenshteĭn
Biochimica Et Biophysica Acta|November 23, 1988
pH-dependence of photo-induced electron transfer in zinc-substituted sperm whale myoglobinA C Shosheva, P K Christova, B P Atanasov
Biochimica Et Biophysica Acta|July 27, 1970
Haem hydration and displacement in the pre-denaturational conformational transition of the myoglobin moleculeA Derzhanski, A Georgieva, K Kotev, et al.
Molecular Biology|January 1, 1972
Calorimetric investigations on heat denaturation of cyanmetmyoglobinB P Atanasov, P L Privalov, N N Khechinashvili
Molekuliarnaia Biologiia|January 1, 1982
[Electron transfer in hemoproteins. VIII. Influence of ionic strength on the rate of reduction of ferricytochrome c by oxymyoglobin derivatives, chemically modified at histidine residues]G B Postnikova, E A Shliapnikova, B P Atanasov, et al.
Molekuliarnaia Biologiia|May 1, 1975
[Selected carboxymethylation of ferri-hemoglobin from insect larvae Chironomus thummi thummi]R I Artoiukh, B P Atanasov, M V Vol'kenshteĭn, et al.
Molekuliarnaia Biologiia|May 1, 1981
[Electron transfer in hemoproteins. VI. The dependence of the reduction rate of ferricytochrome c by oxymyoglobin on ionic strength]G B Postnikova, E A Shliapnikova, M V Vol'kenshteĭn, et al.
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