Zobrazeno 1 - 10
of 141
pro vyhledávání: '"Max A. Lauffer"'
Autor:
Max A. Lauffer
Publikováno v:
Biophysical journal. 58(6)
Biophysics has never been adequately defined. It was my hope when I assumed the editorship of the Biophysical Journal in 1969 that I could make the Journal an instrument for defining the field. To my sorrow, Biophysics is still undefined in 1990. Why
Publikováno v:
Advances in Enzymology-and Related Areas of Molecular Biology ISBN: 9780470122549
Advances in Enzymology and Related Areas of Molecular Biology, Volume 9
Advances in Enzymology and Related Areas of Molecular Biology, Volume 9
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e601cd38e576d098993647ed6090c470
https://doi.org/10.1002/9780470122549.ch4
https://doi.org/10.1002/9780470122549.ch4
Autor:
Max A. Lauffer
Publisher Summary This chapter presents the personal experiences of Max A. Lauffer. As a child and teenager, Lauffer participated actively in the work of the farm. This interest was so strong that, after retirement, Lauffer returned to the farm of hi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::87574190e4695167f4c305cf63ec5270
https://doi.org/10.1016/s0069-8032(00)41008-9
https://doi.org/10.1016/s0069-8032(00)41008-9
Publikováno v:
Archives of Biochemistry and Biophysics. 218:384-401
The effects of absolute temperature (T), ionic strength (μ), and pH on the polymerization of tobacco mosaic virus protein from the 4 S form (A) to the 20 S form (D) were investigated by the method of sedimentation velocity. The loading concentration
Autor:
Max A. Lauffer, Warren H. Gallagher
Publikováno v:
Journal of Molecular Biology. 170:905-919
Calcium ion titrations were performed on solutions of tobacco mosaic virus using a calcium-specific ion-exchange electrode. Scatchard analyses were used to obtain the number of calcium ion binding sites per protein subunit (n) and the apparent stabil
Autor:
Ragaa A. Shalaby, Max A. Lauffer
Publikováno v:
Archives of Biochemistry and Biophysics. 223:224-234
When tobacco mosaic virus (TMV) protein is polymerized at pH values above 7 in unbuffered solutions, either by raising temperature at constant ionic strength or by increasing ionic strength at constant temperature, a 20 S component is formed having b
Autor:
Ragaa A. Shalaby, Max A. Lauffer
Publikováno v:
Archives of Biochemistry and Biophysics. 242:478-487
The effect of the dipolar ions, glycine, glycylglycine, and glycylglycylglycine on the polymerization of tobacco mosaic virus (TMV) protein has been studied by the methods of light scattering and ultracentrifugation. All three dipolar ions promote po
Autor:
Ragaa A. Shalaby, Max A. Lauffer
Publikováno v:
Archives of Biochemistry and Biophysics. 201:224-234
The entropy-driven polymerization of tobacco mosaic virus protein is favored by an increase in ionic strength, μ, and by a decrease in pH. The effect of ionic strength is interpreted in terms of salting-out and electrical work, a function of charge
Autor:
Max A. Lauffer, Ragaa A. Shalaby
Publikováno v:
Archives of Biochemistry and Biophysics. 204:494-502
Protein of the tobacco mosaic virus mutant E66 has lysine replacing asparagine of the type strain, vulgare, at position 140. Thus, E66 protein should have one more positive or one less net negative charge than vulgare at pH 6 to 7. To investigate the
Autor:
Ross Aiken Gortner, Max A. Lauffer
Publikováno v:
The Journal of Physical Chemistry. 43:721-732