Structure of single-stranded virus RNA in situ

Добров, Е. Н.; Kust, S. V.; Yakovleva, Oksana; Tikchonenko, T.I.

doi:10.1016/0005-2787(77)90323-9

Cited by 17 publications

(8 citation statements)

References 29 publications

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“…The CP preparations were stored at concen trations of 4 to 5 mg/ml in 5 mM Na/Na phosphate buffer (PB), pH 8.0, at 4 or -20°C. The protein concen tration was measured by UV spectroscopy using the extinction coefficient Е 280 0,1% of 1.30 [13]. UV spectroscopy.…”

Section: Purification Of Viruses and Cp Preparationmentioning

confidence: 99%

Low sodium dodecyl sulfate concentrations inhibit tobacco mosaic virus coat protein amorphous aggregation and change the protein stability

Rafikova

Panyukov

Arutyunyan

et al. 2004

Biochemistry (Moscow)

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Effects of low SDS concentrations on amorphous aggregation of tobacco mosaic virus (TMV) coat protein (CP) at 52 degrees C and on the protein structure were studied. It was found that SDS completely inhibits the TMV CP (11.5 microM) unordered aggregation at the detergent/CP molar ratio of 15 : 1 (0.005% SDS). As judged by fluorescence spectroscopy, these SDS concentrations did not prevent heating-induced disordering of the large-distance part of the TMV CP subunit, including the so-called "hydrophobic girdle". At somewhat higher SDS/protein ratio (40 : 1) the detergent completely disrupted the TMV CP hydrophobic girdle structure even at room temperature. At the same time, these low SDS concentrations (15 : 1, 40 : 1) strongly stabilized the structure of the small-distance part of the TMV CP molecule (the four alpha-helix bundle) against thermal disordering as judged by the far-UV (200-250 nm) CD spectra. Possible mechanisms of TMV CP heating-induced unordered aggregation initiation are discussed.

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Section: Purification Of Viruses and Cp Preparationmentioning

confidence: 99%

Low sodium dodecyl sulfate concentrations inhibit tobacco mosaic virus coat protein amorphous aggregation and change the protein stability

Rafikova

Panyukov

Arutyunyan

et al. 2004

Biochemistry (Moscow)

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“…Samsun plants. The viruses were purified by chloroform-butanol treatment, polyethylene glycol precipitation and several cycles of differential centrifugation [11].…”

Section: Virus Growth and Purification And Preparation ()F Virus Coatmentioning

confidence: 99%

“…The concentrations of intact viruses, A-proteins and RPs were determined by UV spectroscopy using the following coefficients: E. _, G0 ~lW =2.30 for intact viruses and E~s0 ~1~ = 1.30 for A-proteins and RPs of both viruses [11]. For light-scattering suspensions of intact viruses and RPs true values of absorption determined by the extrapolation method [11] were used in calculations.…”

Section: Virus Growth and Purification And Preparation ()F Virus Coatmentioning

confidence: 99%

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A comparative differential scanning calorimetric study of tobacco mosaic virus and of its coat protein ts mutant

et al. 1998

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The differential scanning calorimetry (DSC) 'melting curves' for virions and coat proteins (CP) of wild-type tobacco mosaic virus (strain UI) and for its CP ts mutant ts21-66 were measured. Strain UI and ts21-66 mutant (two amino acid substitutions in CP: I21 ~ T and D66 ~ G) differ in the type of symptoms they induce on some host plants. It was observed that CP subunits of both U1 and ts21-66 at pH 8.0, in the form of small (3-4S) aggregates, possess much lower thermal stability than in the virions. Assembly into the virus particles resulted in a DSC melting temperature increase from 41 to 72°C for UI and from 38 to 72°C for ts21-66 CP. In the RNA-free helical viruslike protein assemblies UI and ts21-66 CP subunits had a thermal stability intermediate between those in 3--4S aggregates and in the virions, ts21-66 helical protein displayed a somewhat lower thermal stability than U1.

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“…The CP preparations were stored at concentrations of 4.5–6 mg · mL −1 (259–345 × 10 −6 M ) in 10 × 10 −3 M Na + /Na + phosphate buffer (PB), pH 8.0, at 4 ° or −20 °C. The TMV CP concentrations were measured with a dual‐beam spectrophotometer (Shimadzu UV‐1601) using a 1‐cm cuvette, given the molar absorbance coefficient ε at 280 nm of 1.30 32. Non‐ionic surfactant Triton® X‐100a and anionic SDS were purchased from Sigma.…”

Section: Experimental Partmentioning

confidence: 99%

Surfactant‐Induced Amorphous Aggregation of Tobacco Mosaic Virus Coat Protein: A Physical Methods Approach

Panyukov

Nemykh

Добров

et al. 2008

Macromolecular Bioscience

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The interactions of non-ionic surfactant Triton X-100 and the coat protein of tobacco mosaic virus, which is an established model for both ordered and non-ordered protein aggregation, were studied using turbidimetry, differential scanning calorimetry, isothermal titration calorimetry, and dynamic light scattering. It was found that at the critical aggregation concentration (equal to critical micelle concentration) of 138 x 10(-6) M, Triton X-100 induces partial denaturation of tobacco mosaic virus coat protein molecules followed by protein amorphous aggregation. Protein aggregation has profound ionic strength dependence and proceeds due to hydrophobic sticking of surfactant-protein complexes (start aggregates) with initial radii of 46 nm. It has been suggested that the anionic surfactant sodium dodecyl sulfate forms mixed micelles with Triton X-100 and therefore reverses protein amorphous aggregation with release of protein molecules from the amorphous aggregates. A stoichiometric ratio of 5 was found for Triton X-100-sodium dodecyl sulfate interactions.

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Structure of single-stranded virus RNA in situ

Cited by 17 publications

References 29 publications

Low sodium dodecyl sulfate concentrations inhibit tobacco mosaic virus coat protein amorphous aggregation and change the protein stability

Low sodium dodecyl sulfate concentrations inhibit tobacco mosaic virus coat protein amorphous aggregation and change the protein stability

A comparative differential scanning calorimetric study of tobacco mosaic virus and of its coat protein ts mutant

Surfactant‐Induced Amorphous Aggregation of Tobacco Mosaic Virus Coat Protein: A Physical Methods Approach

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