Abstract：
:Twenty-five different temperature-sensitive point mutations at 20 sites in the lysozyme gene of bacteriophage T4 have been identified. All of the mutations alter amino acid side chains that have lower than average crystallographic thermal factors and reduced solvent accessibility in the folded protein. This suggests that the amino acids with well-defined conformations can form specific intramolecular interactions that make relatively large contributions to the thermal stability of the protein. Residues with high mobility or high solvent accessibility are much less susceptible to destabilizing substitutions, suggesting that, in general, such amino acids contribute less to protein stability. The pattern of the sites of ts substitutions observed in the folded conformation of T4 lysozyme suggests that severe destabilizing mutations that primarily affect the free energy of the unfolded state are rare. These results indicate that proteins can be stabilized by adding new interactions to regions that are rigid or buried in the folded conformation.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Alber T,Sun DP,Nye JA,Muchmore DC,Matthews BWdoi
10.1021/bi00387a002subject
Has Abstractpub_date
1987-06-30 00:00:00pages
3754-8issue
13eissn
0006-2960issn
1520-4995journal_volume
26pub_type
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