期刊
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS
卷 88, 期 9, 页码 1189-1196出版社
WILEY
DOI: 10.1002/prot.25890
关键词
molecular dynamics; protein engineering; rational design
资金
- NIST, Innovation in Measurement Science Award
- Summer Undergraduate Research Fellowship [70NANB18H153]
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.
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