A polar, solvent-exposed residue can be essential for native protein structure.

ABSTRACT:

Background

A large energy gap between the native state and the non-native folded states is required for folding into a unique three-dimensional structure. The features that define this energy gap are not well understood, but can be addressed using de novo protein design. Previously, alpha(2)D, a dimeric four-helix bundle, was designed and shown to adopt a native-like conformation. The high-resolution solution structure revealed that this protein adopted a bisecting U motif. Glu7, a solvent-exposed residue that adopts many conformations in solution, might be involved in defining the unique three-dimensional structure of alpha(2)D.

Results

A variety of hydrophobic and polar residues were substituted for Glu7 and the dynamic and thermodynamic properties of the resulting protein

SUBMITTER: Hill RB 

PROVIDER: S-EPMC3050062 | biostudies-literature | 2000 May

REPOSITORIES: biostudies-literature