Effects of Increased Loop Flexibility on the Structure and Stability of a De Novo Designed Helical Protein.

Title: Effects of Increased Loop Flexibility on the Structure and Stability of a De Novo Designed Helical Protein.

Volume: 8 Issue: 2

Author(s): Brigtte Simons, Dean Scholl, Terry Cyr and Mary Alice Hefford

Affiliation:

Keywords: de novo protein, mb-1, mb-16

Abstract: MB-1 is a de novo protein designed to incorporate amino acids required for dairy cow nutrition while folding into a four-helix-bundle. Analysis shows that, as per design, MB-1 is a largely helical protein but appears to be dimeric and shows less stability than expected. Recent evidence indicates that the loop regions in MB-1 may have been under-designed. The variant, MB-16, described here attempts to correct potentially detrimental effects on turn formation by introducing a flexible, five-glycine residues sequence as the second loop.

Cite this article as:

Simons Brigtte, Scholl Dean, Cyr Terry and Hefford Alice Mary, Effects of Increased Loop Flexibility on the Structure and Stability of a De Novo Designed Helical Protein., Protein & Peptide Letters 2001; 8 (2) . https://dx.doi.org/10.2174/0929866013409580