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The thermal stability of immunoglobulin: unfolding and aggregation of a multi-domain protein
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The conformations, which are drawn at random from the ensembles, are oriented in the principle axis frames to illustrate the average prolate ellipsoidal shape as well as the large fluctuations that characterize the conformational distributions
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Can the differences quantified in Fig
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Conversely, zooming out or scaling up from the contact density map of a short protein like PSBD will yield the contact density maps of longer proteins such as ubiquitin or titin
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The key to solving the protein-folding problem lies in an accurate description of the denatured state
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We now proceed onto a discussion of the role of flux, solder bath temperature, and surface interfacial tensions on the wettability evaluation of Sn-2
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© 2005 by the Biophysical Society0006-3495/05/01/172/12 $2
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) puts all nonproprietary information related to the milk genome on the Internet
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. coelicolor has been reported, and the corresponding proteins cloned and expressed (14-16)
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. Rho GTPases are molecular switches, cycling between inactive (guanosine diphosphate-bound) and active (guanosine triphosphate-bound) configurations
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.Thus, the relationship between thermal atomic fluctuations and functionally important motions is not straightforward
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. Therefore, correlating the wetting balance tests results and the morphological analysis, it can be concluded that the higher soldering temperature enhances the wettability due to the rapid chemical reactions between the solder and the substrate
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. At this pH the protein has a net negative charge, the dimer carrying a charge of -17e (36), where e is the protonic charge; and so the apparent specific volume would be expected to have a contribution from net repulsive electric double layer interactions in addition to the excluded volume of the hydrated protein itself
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. The pellets cultured in DMEM/10%FCS were highly compacted without any obvious spacious matrix (Fig
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