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Modeling microdomains: The surface area of globin helices
Author(s) -
Weaver David L.
Publication year - 1992
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.340130405
Subject(s) - helix (gastropod) , folding (dsp implementation) , surface (topology) , globin , diffusion , resolution (logic) , crystallography , materials science , biophysics , chemistry , chemical physics , physics , hemoglobin , thermodynamics , computer science , geometry , mathematics , biology , biochemistry , engineering , ecology , snail , electrical engineering , artificial intelligence
The accessible surface areas of 53 high‐resolution globin helices are correlated with molecular weight. The linear fit is assessed for satistical accuracy using a boot‐strap analysis, and by comparison to the areas of 13 ideal polyalanine α‐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. © 1992 Wiley‐Liss, Inc.