Multiple Methionine Substitutions are Tolerated in T4 Lysozyme and have Coupled Effects on Folding and Stability
(MSE)NIFE(MSE)LRIDEGLRLKIYKDTEGYYTIGIGHLLTKSPSLNAAKSELDKAIGRNTNGVITKDEAEKLFNQDVD AAVRGILRNAK(MSE)KP(MSE)YDS(MSE)DAVRRAA(MSE)IN(MSE)VFQ(MSE)GETR(MSE)AGFTNS(MSE)R (MSE)(MSE)QQKRWDEAAVN(MSE)AKSRWYNQTPNRAKRVITT(MSE)RTGTWDAYKNL
MNIFEMLRIDEGLRLKIYKDTEGYYTIGIGHLLTKSPSLNAAKSELDKAIGRNTNGVITKDEAEKLFNQDVDAAVRGILR NAKMKPMYDSMDAVRRAAMINMVFQMGETRMAGFTNSMRMMQQKRWDEAAVNMAKSRWYNQTPNRAKRVITTMRTGTWDA YKNL
T4 lysozyme with mutations C54T/L84M/V87M/L91M/C97A/L99M/V111M/L118M/L121M/L133M
Residues ASN 163 and LEU 164 are missing in the electron density.
hydrolase (o-glycosyl), T4 lysozyme, methionine core mutant, protein engineering, protein folding, HYDROLASE
MNIFEMLRIDEGLRLKIYKDTEGYYTIGIGHLLTKSPSLNAAKSELDKAIGRNCNGVITKDEAEKLFNQDVDAAVRGILR NAKLKPVYDSLDAVRRCALINMVFQMGETGVAGFTNSLRMLQQKRWDEAAVNLAKSRWYNQTPNRAKRVITTFRTGTWDA YKNL