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

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

Journal Name: Protein & Peptide Letters

Volume 8 , Issue 2 , 2001

Become EABM
Become Reviewer

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.

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

Rights & PermissionsPrintExport Cite as


Article Details

VOLUME: 8
ISSUE: 2
Year: 2001
Page: [89 - 96]
Pages: 8
DOI: 10.2174/0929866013409580
Price: $58

Article Metrics

PDF: 3