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Updated: Aug 21, 2026

Assessment of Immunologically Relevant Dynamic Tertiary Structural Features of the HIV-1 V3 Loop Crown R2 Sequence by ab initio Folding
Published on: September 15, 2010
The folding of spectrin domains II: phi-value analysis of R16
Kathryn A Scott1, Lucy G Randles, Jane Clarke
1MRC Centre for Protein Engineering, University of Cambridge Chemical Laboratory, Lensfield Road, Cambridge CB2 1EW, UK.
Abstract:
Studies on the folding of helical proteins have shown a wide range of different mechanisms and highlighted the importance of helical propensity as a factor in determining folding mechanism. Here, we contribute to this interesting field with the protein engineering phi-value analysis of the 16th domain of chicken brain alpha-spectrin, R16. The fortuitous curvature seen in the unfolding arm of the chevron plot allows us to investigate both early and late events in folding. R16 is the first two-state helical protein for which this has been possible.
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