Triple Point Mutation Asp10 → His, Asn101 → Asp, Argl48 → Ser in T4 Phage Lysozyme Leads to the Molten Globule
Document Type
Article
Publication Date
1992
Digital Object Identifier (DOI)
https://doi.org/10.1093/protein/5.8.781
Abstract
The triple amino acid replacement (Asp10 → His, Asn101 → Asp, Arg148 → Ser) in T4 phage lysozyme was carried out by site-directed mutagenesis. At acid pH (2.7) the mutant is in a confonnational state with the properties of the molten globule: (i) the mutant protein molecule is essentially compact; (ii) its CD spectrum in the near UV region is drastically reduced in intensity as compared with the wild type protein spectrum; (iii) the CD spectrum in the far UV region indicates the presence of pronounced secondary structure in the mutant; (iv) unlike the wild type protein the mutant protein can bind the hydrophobic fluorescent probe, ANS.
Was this content written or created while at USF?
Yes
Citation / Publisher Attribution
Protein Engineering, Design and Selection, v. 5, issue 8, p. 781-783
Scholar Commons Citation
Uversky, Vladimir N.; Leontiev, Vladimir V.; and Gudkov, Anatoly T., "Triple Point Mutation Asp10 → His, Asn101 → Asp, Argl48 → Ser in T4 Phage Lysozyme Leads to the Molten Globule" (1992). Molecular Medicine Faculty Publications. 620.
https://digitalcommons.usf.edu/mme_facpub/620
