Polarographic Changes Accompanying the Re-Formation of Tobacco Mosaic Virus Capsid from Its Disordered Polypeptide Chains

Ruttkay-Nedecký, G; Bezúch, B.

doi:10.1007/978-3-0348-5848-9_53

Cited by 11 publications

(1 citation statement)

References 16 publications

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“…Polarographic data for L-ascorbic acid and erythorbic acid after exposure to air (918) and for scorbamic acid which was compared to ascorbic acid (579) were discussed. Polarographic changes as the results of denaturation and renaturation of tobacco mosaic virus protein were investigated (780). The effect of powerful irritants and biologically active substances on the level of serum sulfhydryl groups (482), energy functions of dog lung mitochondria (212), the activity of succinate oxidase from new born rat brain mitochondria (973), and the kinetics of a thiamine reaction in base solution (948) were examined polarographically.…”

Section: Biological-pharmaceutical Studiesmentioning

confidence: 99%

Organic polarography

Pietrzyk¹

1972

Anal. Chem.

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Section: Biological-pharmaceutical Studiesmentioning

confidence: 99%

Organic polarography

Pietrzyk¹

1972

Anal. Chem.

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Adsorption behaviour of globular proteins at the water/mercury interface

Scheller¹,

Jänchen²,

Prümke³

1975

Biopolymers

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SynopsisThe adsorption of globular proteins a t solidhiquid or liquidhiquid interfaces provides evidence of unfolded molecular conformation. Proteins with high apolar character are strongly unfolded, while those with high polar character are generally incompletely unfolded. Structural changes of globular proteins a t adsorption on mercury electrodes were studied by ac polarography and capacity-time curves. The surface area per molecule of nine globular proteins was determined from the adsorption kinetics a t the dropping mercury electrode. For all the proteins investigated, this value was greater than the maximal molecular cross section of the native proteins. The surface area was about 19 Az per amino acid residue, which coincides with the value for unfolded proteins a t the water/air interface. Differences between dropping mercury electrode and hanging drop mercury electrode occurred only with lysozyme and phosphorylase; for the other proteins, the structure of the adsorption layer was independent of the time of interaction at the electrode. Since not all of the reducible groups of the adsorbed proteins come into contact with the electrode, the flattening should be incomplete.

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Electrochemistry of Biopolymers

Berg

1985

Comprehensive Treatise of Electrochemistry

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Polarographic Changes Accompanying the Re-Formation of Tobacco Mosaic Virus Capsid from Its Disordered Polypeptide Chains

Cited by 11 publications

References 16 publications

Organic polarography

Organic polarography

Adsorption behaviour of globular proteins at the water/mercury interface

Electrochemistry of Biopolymers

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