|Title||Globularity and protein function.|
|Publication Type||Journal Article|
|Year of Publication||2000|
|Journal||J Biomol Struct Dyn|
|Volume||17 Suppl 1|
|Keywords||Hydrophobic and Hydrophilic Interactions, Protein Conformation, Protein Folding, Protein Structure, Secondary, Protein Structure, Tertiary, Proteins|
Abstract The forces that direct protein folding lead naturally to native proteins and protein domains that are typically, to a first approximation, globular-spherical and compact, with a relatively clear distinction between the hydrophobic inside and polar outside. The near-universality of these features of protein structures sharpens our focus on some apparent exceptions. Consideration of the structure/function link in some of the exceptional cases provides some insights into our views of protein function.
|Alternate Journal||J. Biomol. Struct. Dyn.|