A. Messerschmidt, X-Ray Crystallography of Biomacromolecules: A Practical Guide, Wiley-VCH, Weinheim, Germany (2007) xiii + 304 pp., £119.00, ISBN: 3-527-31396-9.
- 作者：Katarzyna Bunko ; John F. Kennedy
- 关键词：Protein aggregation ; Beta sheet ; Hetero-aggregation ; Fluorescence ; Confocal ; Retro-proteins
- 刊名：International Journal of Biological Macromolecules
- 出版年：2007
- 期刊代码：62_01418130
- 类别：abs
- 出版时间：1 December 2007
- 卷：41
- 期：5
- 页码：656-657
- 文件大小：46 K
摘要
Can two unrelated proteins with deliberately compromised folding abilities, marked propensities to aggregate upon increase of protein concentration, and proclivities towards beta sheet formation, be caused to hetero-aggregate? We address this question here using the ‘designer’ backbone-reversed forms of two model all-beta sheet proteins, E. coli CspA and C. elegans HSP12.6, both earlier created and characterized by our group. These were covalently labeled with fluorescent dyes of well-resolved spectral characteristics [retro-CspA with FITC, and retro-HSP12.6 with TRITC] and then allowed to aggregate within the same reaction vessel. The resultant aggregates are shown by spectrofluorimetry-coupled confocal laser scanning microscopy to constitute uniform mixtures of both proteins, existing within every cylindrical volume element of ≈200 nm diameter, and comparable height, in all sections of the co-aggregated material suggesting that the two proteins do not selectively associate with copies of themselves during aggregation. Thus, it would appear that aggregation can occur without reference to protein molecular identity.