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Comparing wild\u2010type protein and mutant Ni 2068 (Tyr\u2010139\u2192Cys\u2010139) a tentative localization of aromatic amino acids in the threedimensional structure is rendered possible.<\/jats:p><jats:p>In all modes of aggregation the CD spectra are determined by intrasubunit interactions between aromatic residues, in particular Trp\u201017 and Trp\u201052 as well as Tyr\u201070, Tyr\u201072 and Tyr\u2010139. The Trp\u20101 7Trp\u201052 interaction was found to be highly sensitive towards changes of the quaternary structure especially with respect to helical aggregates. This suggests that the environment of the two tryptophan residues is of crucial importance in the three\u2010dimensional structure of the subunit; in the course of aggregation intersubunit interactions compete with the specific intrasubunit Trp\u201017\u2010Trp\u201052 interactions.<\/jats:p><jats:p>It is suggested that Tyr\u201070 and Tyr\u201072 form hydrogen bonds in a strongly hydrophobic environment. Formation of the double disc decreases the rotatory strength, pointing to an increase in conformational flexibility.<\/jats:p><jats:p>Spectroscopic and chemical evidence prove that Tyr\u201070, Tyr\u201072 and Tyr\u2010139 are in close neighbourhood. Double disc formation by lowering the pH (pH 8 \u2192 6.9, I = 0.1 M) or increasing the ionic strength (pH 8, I = 0.1 \u2192 0.6 M) is reflected by identical spectral effects in the environment of Tyr\u201070\u2010Tyr\u201072. However the interaction between Trp\u201017 and Trp\u201052 indicates significant differences in the conformation which may be important for the formation of higher aggregates, i.e. \u2018lockwashers\u2019, helices, and \u2018stacked discs\u2019.<\/jats:p>","DOI":"10.1111\/j.1432-1033.1976.tb10036.x","type":"journal-article","created":{"date-parts":[[2005,3,3]],"date-time":"2005-03-03T16:28:32Z","timestamp":1109867312000},"page":"423-431","source":"Crossref","is-referenced-by-count":13,"title":["Circular\u2010Dichroism and Absorption Spectroscopic Studies on Specific Aromatic Residues Involved in the Different Modes of Aggregation of Tobacco\u2010Mosaic\u2010Virus Protein"],"prefix":"10.1111","volume":"61","author":[{"given":"Dieter","family":"VOGEL","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Rainer","family":"JAENICKE","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2008,6,28]]},"reference":[{"key":"e_1_2_2_2_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0065-3233(08)60268-5"},{"key":"e_1_2_2_3_2","first-page":"149","volume-title":"Biological Macromolecules","author":"Lauffer M. 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