Journal
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS
Volume 88, Issue 9, Pages 1189-1196Publisher
WILEY
DOI: 10.1002/prot.25890
Keywords
molecular dynamics; protein engineering; rational design
Categories
Funding
- NIST, Innovation in Measurement Science Award
- Summer Undergraduate Research Fellowship [70NANB18H153]
Ask authors/readers for more resources
ClpS2 is a small protein under development as a probe for selectively recognizing N-terminal amino acids of N-degron peptide fragments. To understand the structural basis of ClpS2 specificity for an N-terminal amino acid, all atom molecular dynamics (MD) simulations were conducted using the sequence of a bench-stable mutant of ClpS2, called PROSS. We predicted that a single amino acid leucine to asparagine substitution would switch the specificity of PROSS ClpS2 to an N-terminal tyrosine over the preferred phenylalanine. Experimental validation of the mutant using a fluorescent yeast-display assay showed an increase in tyrosine binding over phenylalanine, in support of the proposed hypothesis.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available