A T Gudkov - JoVE Visualize

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Biofizika|July 1, 1993

[The effect of point amino acid substitutions on T4 phage lysozyme stability. II. Transition of a protein molecule to the "molten globule" state with replacements Asp10---His, Asn101---Asp, Arg148---Ser]V V Leont'ev, V N Uverskiĭ, O I Griaznova, et al.

FEBS Letters|March 3, 1986

Structure of protein-deficient 50 S ribosomal subunits. Particles without 5 S RNA-protein complex retain the L7/L12 stalk and associate with 30 S subunitsO M Selivanova, G M Gongadze, A T Gudkov, et al.

FEBS Letters|June 27, 1983

Physical properties of ribosomal proteins isolated under different conditions from the Escherichia coli 50 S subunitL G Tumanova, G M Gongadze, Venyaminov SYu, et al.

Journal of Molecular Biology|October 31, 2000

Structure of a mutant EF-G reveals domain III and possibly the fusidic acid binding siteM Laurberg, O Kristensen, K Martemyanov, et al.

Protein Expression and Purification|April 3, 2001

Cell-free production of biologically active polypeptides: application to the synthesis of antibacterial peptide cecropinK A Martemyanov, V A Shirokov, O V Kurnasov, et al.

Molekuliarnaia Biologiia|January 1, 1984

[Structure and density of ribosomal RNA and its complexes with proteins in a solution]I N Serdiuk, S Ch Agalarov, G M Gongadze, et al.

Molekuliarnaia Biologiia|May 1, 1984

[Comparison of the physical properties of ribosomal proteins from Escherichia coli 50S subparticles isolated by different methods]L G Tumanova, G M Gongadze, S Iu Ven'iaminov, et al.

Protein Science : a Publication of the Protein Society|September 1, 1996

Circularly permuted dihydrofolate reductase possesses all the properties of the molten globule state, but can resume functional tertiary structure by interaction with its ligandsV N Uversky, V P Kutyshenko, Protasova NYu, et al.

Protein Engineering|November 1, 1994

Circularly permuted dihydrofolate reductase of E. coli has functional activity and a destabilized tertiary structureProtasova NYu, M L Kireeva, N V Murzina, et al.

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Showing results (41-50 of 49) with videos related to

Sort By:

Pageof 5

You have reached the last page of results.This site can display upto 49 results.

Biofizika|July 1, 1993

[The effect of point amino acid substitutions on T4 phage lysozyme stability. II. Transition of a protein molecule to the "molten globule" state with replacements Asp10---His, Asn101---Asp, Arg148---Ser]V V Leont'ev, V N Uverskiĭ, O I Griaznova, et al.

FEBS Letters|March 3, 1986

Structure of protein-deficient 50 S ribosomal subunits. Particles without 5 S RNA-protein complex retain the L7/L12 stalk and associate with 30 S subunitsO M Selivanova, G M Gongadze, A T Gudkov, et al.

FEBS Letters|June 27, 1983

Physical properties of ribosomal proteins isolated under different conditions from the Escherichia coli 50 S subunitL G Tumanova, G M Gongadze, Venyaminov SYu, et al.

Journal of Molecular Biology|October 31, 2000

Structure of a mutant EF-G reveals domain III and possibly the fusidic acid binding siteM Laurberg, O Kristensen, K Martemyanov, et al.

Protein Expression and Purification|April 3, 2001

Cell-free production of biologically active polypeptides: application to the synthesis of antibacterial peptide cecropinK A Martemyanov, V A Shirokov, O V Kurnasov, et al.

Molekuliarnaia Biologiia|January 1, 1984

[Structure and density of ribosomal RNA and its complexes with proteins in a solution]I N Serdiuk, S Ch Agalarov, G M Gongadze, et al.

Molekuliarnaia Biologiia|May 1, 1984

[Comparison of the physical properties of ribosomal proteins from Escherichia coli 50S subparticles isolated by different methods]L G Tumanova, G M Gongadze, S Iu Ven'iaminov, et al.

Protein Science : a Publication of the Protein Society|September 1, 1996

Circularly permuted dihydrofolate reductase possesses all the properties of the molten globule state, but can resume functional tertiary structure by interaction with its ligandsV N Uversky, V P Kutyshenko, Protasova NYu, et al.

Protein Engineering|November 1, 1994

Circularly permuted dihydrofolate reductase of E. coli has functional activity and a destabilized tertiary structureProtasova NYu, M L Kireeva, N V Murzina, et al.

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