Modeling microdomains: the surface area of globin helices.
The accessible surface areas of 53 high-resolution globin helices are correlated with molecular weight. The linear fit is assessed for statistical accuracy using a boot-strap analysis, and by comparison to the areas of 13 ideal polyalanine alpha-helices. The accessible area of the unfolded helices is compared with the folded values before helix-helix packing. An analytical physical model is presented to explain the correlation, and to provide an analytical value for the surface area parameter in the diffusion-collision model of protein folding.
Weaver
D L
DL
Department of Physics, Tufts University, Medford, Massachusetts 02155.
D000818:Animals; D005914:Globins / Q000737:chemistry*; D006801:Humans; D007700:Kinetics; D008432:Mathematical Computing; D008956:Models, Chemical; D011487:Protein Conformation; D013499:Surface Properties
D005914:Globins