title: Triple point mutation Asp10-->His, Asn101-->Asp, Arg148-->Ser in T4 phage lysozyme leads to the molten globule.
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 conformational 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.
authors.affiliation: Institute of Protein Research, Academy of Sciences of Russia, Pushchino, Moscow Region.
authors.forename: V N
authors.initials: VN
authors.lastname: Uversky
authors.forename: V V
authors.initials: VV
authors.lastname: Leontiev
authors.forename: A T
authors.initials: AT
authors.lastname: Gudkov
mesh_terms: D017122:Bacteriophage T4 / Q000201:enzymology* / Q000235:genetics; D002942:Circular Dichroism; D005456:Fluorescent Dyes; D009113:Muramidase / Q000737:chemistry* / Q000235:genetics; D016297:Mutagenesis, Site-Directed; D011487:Protein Conformation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D013056:Spectrophotometry, Ultraviolet
chemical_list: D005456:Fluorescent Dyes; D009113:Muramidase