Protein unfolding global analysis

G. A. Arteca, O. Nilsson, and O. Tapia,/. Mol. Graphics, 11,193 (1993). Global Characterization of Protein Secondary Structures. Analysis of Computer-Modeled Protein Unfolding. 

The previous section looked at examples in which detailed analysis of specific proteins identified as targets of the heat shock response has led to the identification of new molecular chaperones as well as an expanded view of the requirements for efficient protein production and folding. In this section we focus on how the use of DNA microarrays has provided a global view of the spectrum of targets of a specific stress response, the unfolded protein response (UPR), which plays a critical... 

As stressed many times in this chapter, analysis of the denaturation of globular proteins is a complex problem. In practice, what is generally monitored is the global result of two different processes the conformational transition of the molecule, and the subsequent aggregation of unfolded protein molecules in many cases, the two processes cannot be separated, and this is a first difficulty in the thermodynamical approach. The second level of problems is inherent to the processes themselves considered separately. 

ESI mass spectrum acquired under denaturing conditions (black trace in Figure 10.4) was noticeably higher. This suggests that the solvent accessible surface area of noncompact conformers of NEM-IFN, whose presence under near-native conditions is revealed by the protein ion charge state distribution analysis, is lower compared to the fully denatured species of IFN [3233]. However, this technique yields only a global measure of conformational disorder and, therefore, cannot provide any information that would allow these unfolding events to be localized within the protein structure. 

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