By B C Crandall; James Lewis
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Extra resources for Nanotechnology : research and perspectives : papers from the First Foresight Conference on Nanotechnology
F . . • • . . , , obscured by overlap As an alternative approach to obtaining some information about helix helix packing, we prepared "mutants" of the alB peptide. On the basis of the computer model of the 4-helix bundle, we selected leucine pairs that could be replaced by unique hydrophobic residues such that NOEs between them could be unequivocally attributed to interhelical NOEs. In the first variant, Leu3 and Leu13 were replaced with a valine and a phenylalanine, respectively. Based on our computer model, these residues should be close enough in space to give rise to NOEs if the helices align in an anti parallel orientation (plate 5).
4, which has two sites per bundle, the proton resonances of the six histidine residues are sharp and well defined (figure 3. 10b). Thus it appears that two occupied sites create a more structured and less dynamic bundle than bundles with only one occupied site or those without any metal ions at all. This illustrates the additive nature of specific interactions in structuring these bundles. The conformational stability of the peptides in the presence and ab sence of Zn +2 was assessed by circular dichroism.
Designing functional helical bundles. 1 Incremental strategy for designing the 4-helix bundle. functions. For example, in the case of the 4-helix bundles, we are inter ested in making metal-binding 4-helix bundles that can perform inter esting catalytic or redox chemistry, or bundles that can fold and unfold in response to chemical stimuli. Ultimately we want to understand more than just how to make helical proteins. A Holy Grail of structural biology is to understand all of the determinants of protein folding so that we can create proteins that are complex, multi domain, and impressive in functionality.