The folding of spectrin domains II: phi-value analysis of R16.


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. Study holds ProTherm entries: 18107, 18108, 18109, 18110, 18111, 18112, 18113, 18114, 18115, 18116, 18117, 18118, 18119, 18120, 18121, 18122, 18123, 18124, 18125, 18126, 18127, 18128, 18129, 18130, 18131, 18132, 18133, 18134, 18135, 18136, 18137, 18138, 18139, 18140, 18141, 18142, 18143, 18144, 18145, 18146, 18147, 18148, 18149, 18150, 18151, 18152, 18153, 18154, 18155, 18156, 18157, 18158, 18159, 18160, 18161, 18162, 18163, 18164, 18165, 18166, 18167, 18168, 18169, 18170, 18171, 18172, 18173, 18174, 18175 Extra Details: 16th domain. dGH2O is calculated using a mean value of m = 1.9 kcal/mol/M. protein folding; chevron plot; curvature; phi-value; spectrin

Submission Details

ID: PycmqvSn

Submitter: Connie Wang

Submission Date: April 24, 2018, 8:50 p.m.

Version: 1

Publication Details
Scott KA;Randles LG;Clarke J,J. Mol. Biol. (2004) The folding of spectrin domains II: phi-value analysis of R16. PMID:15504412
Additional Information

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