1964
DOI: 10.1515/znb-1964-1010
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Untersuchung des gelösten Tabakmosaikvirus-Proteins mittels der Röntgen-Kleinwinkelstreuung unter Verwendung der Absolutintensität

Abstract: Das Verhalten von TMV-Proteinmolekülen in verschiedenen Lösungsmitteln wurde untersucht. In Essigsäure liegen partiell denaturierte Monomere vom Mol.-Gew. 17 300 vor. In 0,01-n. NaOH bilden sich aus mehreren Monomeren stäbchenförmige Aggregate. In 36-proz. Harnstofflösung wird das TMV-Protein völlig denaturiert. Im Grenzfall unendlicher Verdünnung findet man isotrope monomere Fadenknäuel. Bei höherer Proteinkonzentration lagern sich diese in komplizierter Weise zu Aggregaten zusammen, die bei 2% Proteingehalt … Show more

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Cited by 14 publications
(3 citation statements)
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“…The scattering of the 4-6S A protein, which predominantly contains trimers, is featureless (Figure 4). At 5 °C, the shape of the scattering envelope is virtually independent of protein concentration (up to at least 22 mg/mL) or pH [up to at least pH 12 (Anderer et al, 1964)]. The two-dimensional Guinier region is surprisingly well-defined and yields RG2 = 1.5 nm (Figure 4B), in agreement with the position of the maximum in Figure 4A.…”
Section: Resultssupporting
confidence: 75%
See 1 more Smart Citation
“…The scattering of the 4-6S A protein, which predominantly contains trimers, is featureless (Figure 4). At 5 °C, the shape of the scattering envelope is virtually independent of protein concentration (up to at least 22 mg/mL) or pH [up to at least pH 12 (Anderer et al, 1964)]. The two-dimensional Guinier region is surprisingly well-defined and yields RG2 = 1.5 nm (Figure 4B), in agreement with the position of the maximum in Figure 4A.…”
Section: Resultssupporting
confidence: 75%
“…In addition, the method of obtaining the maximum particle dimension by combination of RG2 and RG3 (Anderer et al, 1964) yields a value of 16 nm which is also inconsistent with a simple native trimer model. The SAXS data thus unambiguously confirm the presence of oligomers larger than trimers, possibly as large as heptamers (Kazel, 1981), that contribute differently at different s vectors.…”
Section: Resultsmentioning
confidence: 97%
“…It seems that about T JL obacco mosaic virus protein may exist in several reversible states of aggregation. Only under particular conditions does the protein occur in monomeric form partially or completely deformed or unfolded (Anderer et al, 1964). Usually it forms a trimer which, through a number of steps is transformed into more complex aggregates and finally by helical arrangement of the subunits to hollow rods (Caspar, 1963;Lauffer and Stevens, 1968).…”
mentioning
confidence: 99%