Transmembrane Helical Protein Folding: Lipid Modulation and Folding Transition States
نویسندگان
چکیده
منابع مشابه
Transition states in protein folding
The folding dynamics of small single-domain proteins is a current focus of simulations and experiments. Many of these proteins are ‘two-state folders’, i.e. proteins that fold rather directly from the denatured state to the native state, without populating metastable intermediate states. A central question is how to characterize the instable, partially folded conformations of two-state proteins...
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The folding reactions of some small proteins show clear evidence of a hierarchic process, whereas others, lacking detectable intermediates, do not. Evidence from folding intermediates and transition states suggests that folding begins locally, and that the formation of native secondary structure precedes the formation of tertiary interactions, not the reverse. Some notable examples in the liter...
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Defining the structural features of a transition state is important in understanding a folding reaction. Here, we use Φ-value and double mutant analyses to probe the folding transition state of the membrane protein bacteriorhodopsin. We focus on the final C-terminal helix, helix G, of this seven transmembrane helical protein. Φ-values could be derived for 12 amino acid residues in helix G, most...
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Nearly a quarter of genomic sequences and almost half of all receptors that are likely to be targets for drug design are integral membrane proteins. Understanding the detailed mechanisms of the folding of membrane proteins is a largely unsolved, key problem in structural biology. Here, we introduce a general model and use computer simulations to study the equilibrium properties and the folding ...
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ژورنال
عنوان ژورنال: Biophysical Journal
سال: 2011
ISSN: 0006-3495
DOI: 10.1016/j.bpj.2010.11.075