The folding of spectrin domains II: phi-value analysis of R16.
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.
Scott
Kathryn A
KA
MRC Centre for Protein Engineering, University of Cambridge Chemical Laboratory, Lensfield Road, Cambridge CB2 1EW, UK.
Randles
Lucy G
LG
Clarke
Jane
J
D000818:Animals; D001923:Brain Chemistry; D002645:Chickens; D004355:Drug Stability; D007700:Kinetics; D008958:Models, Molecular; D016297:Mutagenesis, Site-Directed; D011489:Protein Denaturation; D015202:Protein Engineering; D017510:Protein Folding; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics; D013049:Spectrin / Q000737:chemistry* / Q000235:genetics; D013816:Thermodynamics
D011994:Recombinant Proteins; D013049:Spectrin