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Protein & Peptide Letters


ISSN (Print): 0929-8665
ISSN (Online): 1875-5305

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 and Mary Alice Hefford

Volume 8, Issue 2, 2001

Page: [89 - 96] Pages: 8

DOI: 10.2174/0929866013409580

Price: $65


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

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