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

Authors: Simons B.; Scholl D.; Cyr T.; Hefford M.Alice

Source: Protein and Peptide Letters, Volume 8, Number 2, April 2001 , pp. 89-96(8)

Publisher: Bentham Science Publishers

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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

Language: English

Document Type: Review article

DOI: 10.2174/0929866013409580

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