Substitution with selenomethionine can enhance the stability of methionine-rich proteins.


The availability of a series of phage T4 lysozymes with up to 14 methionine residues incorporated within the protein has made it possible to systematically compare the effect on protein stability of selenomethionine relative to methionine. Wild-type lysozyme contains two fully buried methionine residues plus three more on the surface. The substitution of these methionine residues with selenomethionine slightly stabilizes the protein. As more and more methionine residues are substituted into the protein, there is a progressive loss of stability. This is, however, increasingly offset in the selenomethionine variants, ultimately resulting in a differential increase in melting temperature of about 7 degrees C. This increase, corresponding to about 0.25 kcal/mol per substitution, is in reasonable agreement with the difference in the solvent transfer free energy between the two amino acids. Study holds ProTherm entries: 6062, 6063, 6064, 6065, 6066, 6067 Extra Details: Methionine residues are substituted at M1,M6,M102,M106,M120 structure determination; MAD phasing; T4 lysozyme;,anomalous scattering

Submission Details

ID: PnJkancg3

Submitter: Connie Wang

Submission Date: April 24, 2018, 8:31 p.m.

Version: 1

Publication Details
Gassner NC;Baase WA;Hausrath AC;Matthews BW,J. Mol. Biol. (1999) Substitution with selenomethionine can enhance the stability of methionine-rich proteins. PMID:10556025
Additional Information

Structure view and single mutant data analysis

Study data

No weblogo for data of varying length.
Colors: D E R H K S T N Q A V I L M F Y W C G P

Data Distribution

Studies with similar sequences (approximate matches)

Correlation with other assays (exact sequence matches)

Relevant UniProtKB Entries

Percent Identity Matching Chains Protein Accession Entry Name
100.0 Endolysin P00720 ENLYS_BPT4