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9. A differential scanning calorimetric study of the thermal unfolding of seven mutant forms of phage T4 lysozyme. Connelly P, Ghosaini L, Hu CQ, Kitamura S, Tanaka A, Sturtevant JM. Biochemistry; 1991 Feb 19; 30(7):1887-91. PubMed ID: 1993203 [Abstract] [Full Text] [Related]
11. Replacements of Pro86 in phage T4 lysozyme extend an alpha-helix but do not alter protein stability. Alber T, Bell JA, Sun DP, Nicholson H, Wozniak JA, Cook S, Matthews BW. Science; 1988 Feb 05; 239(4840):631-5. PubMed ID: 3277275 [Abstract] [Full Text] [Related]
16. Amino acid substitutions far from the active site of bacteriophage T4 lysozyme reduce catalytic activity and suggest that the C-terminal lobe of the enzyme participates in substrate binding. Grütter MG, Matthews BW. J Mol Biol; 1982 Jan 25; 154(3):525-35. PubMed ID: 7077670 [No Abstract] [Full Text] [Related]
17. Thermodynamic stability and point mutations of bacteriophage T4 lysozyme. Hawkes R, Grutter MG, Schellman J. J Mol Biol; 1984 May 15; 175(2):195-212. PubMed ID: 6726809 [Abstract] [Full Text] [Related]
18. Thermodynamic effects of proline introduction on protein stability. Prajapati RS, Das M, Sreeramulu S, Sirajuddin M, Srinivasan S, Krishnamurthy V, Ranjani R, Ramakrishnan C, Varadarajan R. Proteins; 2007 Feb 01; 66(2):480-91. PubMed ID: 17034035 [Abstract] [Full Text] [Related]
19. Folding and function of a T4 lysozyme containing 10 consecutive alanines illustrate the redundancy of information in an amino acid sequence. Heinz DW, Baase WA, Matthews BW. Proc Natl Acad Sci U S A; 1992 May 01; 89(9):3751-5. PubMed ID: 1570293 [Abstract] [Full Text] [Related]