Subdomain interactions as a determinant in the folding and stability of T4 lysozyme

Protein Science

Volumn 7, Issue 1, 1998, Pages 96-104

  Llinás, Manuel ^a   Marqusee, Susan ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

Circular permutation; Protein folding; Subdomain; T4 lysozyme

Indexed keywords

LYSOZYME;

ARTICLE; CARBOXY TERMINAL SEQUENCE; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN STABILITY; STRUCTURE ACTIVITY RELATION; THERMODYNAMICS;

EID: 0031891493     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560070110     Document Type: Article

References (44)

1. Alber T. 1989. Mutational effects on protein stability. Anna Rev Biochem 55:765-798.
2. Anderson DE, Becktel WJ, Dahlquist FW. 1990. pH-induced denaturation of proteins: A single salt bridge contributes 3-5 kcal/mol to the free energy of folding of T4 lysozyme. Biochemistry 29:2403-2408.
3. Anderson DE, Lu J, Mclntosh LP, Dahlquist FW. 1993. The folding, stability and dynamics of T4 lysozyme: A perspective using nuclear magnetic resonance. In: Clore GM, Gronenborn AM, eds. NMR of proteins. Boca Raton, Florida: CRC Press. pp 258-304.
4. Brandts JF, Kaplan LJ. 1973. Derivative spectroscopy applied to tyrosyl chromophores. Studies on ribonuclease, lima bean inhibitors, insulin, and pancreatic trypsin inhibitor. Biochemistry 72:2011-2024.
5. Dixon MM, Nicholson H, Shewchuk L, Baase WA, Matthews BW. 1992. Structure of a hinge-bending bacteriophage T4 lysozyme mutant, Ile3 → Pro. J Mol Biol 227:917-933.
6. Edelhoch H. 1967. Spectroscopic determination of tryptophan and tyrosine in proteins. Biochemistry 6:1948-1954.
7. Elwell M, Schellman J. 1975. Phage T4 lysozyme. Physical properties and reversible unfolding. Biochim Biophys Ada 356:309-323.
8. Englander SW, Sosnick TR, Englander JJ, Mayne L. 1996. Mechanisms and uses of hydrogen exchange. Curr Opin Struct Biol 6:18-23.
9. Faber HR, Matthews BW. 1990. A mutant T4 lysozyme displays five different crystal conformations [see comments]. Nature 348:263-266.
10. Heinemann U, Hahn M. 1995. Circular permutation of polypeptide chains: Implications for protein folding and stability. Prog Biophvs Mol Biol 64:121-143.
11. Jaenicke R. 1991. Protein folding: Local structures, domains, subunits, and assemblies. Biochemistry 30:3147-3161.
12. Kim PS, Baldwin RL. 1982. Specific intermediates in the folding reactions of small proteins and the mechanism of protein folding. Anna Rev Biochem 57:459-489.
13. Kuwajima K. 1989. The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure. Proteins Struct Fund Genet 6:87-103.
14. Kuwajima K. 1996. The molten globule state of alpha-lactalbumin. FASEB J 70:102-109.
15. Lu J, Dahlquist FW. 1992. Detection and characterization of an early folding intermediate of T4 lysozyme using pulsed hydrogen exchange and two-dimensional NMR. Biochemistry 57:4749-4756.
16. Matsumura M, Matthews BW. 1989. Control of enzyme activity by an engineered disulfide bond. Science 243:192-194.
17. Matthews BW. 1995. Studies on protein stability with T4 lysozyme. Adv Protein Chem 46:249-278.
18. Matthews BW. 1996. Structural and genetic analysis of the folding and function of T4 lysozyme. FASEB J 10:35-41.
19. McHaourab HS, Lietzow MA, Hideg K, Hubbell WL. 1996. Motion of spin-labeled side chains in T4 lysozyme. Correlation with protein structure and dynamics. Biochemistry 55:7692-7704.
20. McHaourab HS, Oh KJ, Fang CJ, Hubbell WL. 1997. Conformation of T4 lysozyme in solution. Hinge-bending motion and the substrate-induced conformational transition studied by site-directed spin labeling. Biochemistry 36:307-316.
21. McLeish MJ, Nielsen KJ, Najbar LV, Wade JD, Lin F, Doughty MB, Craik DJ. 1994. Conformation of a peptide corresponding to T4 lysozyme residues 59-81 by NMR and CD spectroscopy. Biochemistry 53:11174-11183.
22. McLeish MJ, Nielsen KJ, Wade JD, Craik DJ. 1993. A peptide corresponding to the N-terminal 13 residues of T4 lysozyme forms an alpha-helix. FEBS Lett 315:323-328.
23. Najbar LV, Craik DJ, Wade JD. Lin F, McLeish MJ. 1995. CD and NMR determination of the solution structure of a peptide corresponding to T4 lysozyme residues 38-51. Biochim Biophys Acta 1250:163-170.
24. Nicholson H, Anderson DE. Dao-pin S, Matthews BW. 1991. Analysis of the interaction between charged side chains and the alpha-helix dipole using designed thermostable mutants of phage T4 lysozyme. Biochemistry 30:9816-9828.
25. Oas TG, Kim PS. 1988. A peptide model of a protein folding intermediate. Nature 336:42-48.
26. Peng ZY, Kim PS. 1994. A protein dissection study of a molten globule. Biochemistry 33:2136-2141.
27. Poteete AR, Hardy LW. 1994. Genetic analysis of bacteriophage T4 lysozyme structure and function. J Bacterial 176:6783-6788.
28. Poteete AR, Sun DP, Nicholson H, Matthews BW. 1991. Second-site revenants of an inactive T4 lysozyme mutant restore activity by restructuring the active site cleft. Biochemistry 30:1425-1432.
29. Ptitsyn OB. Pain RH, Semisotnov GV, Zerovnik E, Razgulyaev OI. 1990. Evidence for a molten globule state as a general intermediate in protein folding. FEBS Lett 262:20-24.
30. Radford SE, Dobson CM, Evans PA. 1992. The folding of hen lysozyme involves partially structured intermediates and multiple pathways [see comments]. Mature 355:302-307.
31. Rennell D, Bouvier SE, Hardy LW, Poteete AR. 1991. Systematic mutation of bacteriophage T4 lysozyme. J Mol Biol 222:67-88.
32. Rose GD. 1979. Hierarchic organization of domains in globular proteins. J Mol Biol 134:447-470.
33. Sambrook J, Maniatis T, Fritsch EF. 1989. Molecular cloning: A laboratory manual. Cold Spring Harbor, New York: Cold Spring Harbor Laboratory Press.
34. Santoro MM, Bolen DW. 1988. Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants. Biochemistry 27:8063-8068.
35. Sauer UH, San DP, Matthews BW. 1992. Tolerance of T4 lysozyme to proline substitutions within the long interdomain alpha-helix illustrates the adaptability of proteins to potentially destabilizing lesions. J Biol Chem 267:2393-2399.
36. Schulman BA, Redfield C. Peng ZY. Dobson CM. Kim PS. 1995. Different subdomains are most protected from hydrogen exchange in the molten globule and native states of human alpha-lactalbumin. J Mol Biol 253:651-657.
37. Shoichet BK, Baase WA, Kuroki R, Matthews BW. 1995. A relationship between protein stability and protein function. Proc Natl Acad Sci USA 92:452-456.
38. Staley JP, Kim PS. 1990. Role of a subdomain in the folding of bovine pan-creatic trypsin inhibitor. Nature 344:685-688.
39. Staley JP, Kim PS. 1992. Complete folding of bovine pancreatic trypsin inhibitor with only a single disulfide bond. Proc Natl Acad Sci USA 59:1519-1523.
40. Tsugita A, Inouye M. 1968. Purification of bacteriophage T4 lysozyme. J Biol Chem 243:391-397.
41. Weaver LH, Matthews BW. 1987. Structure of bacteriophage T4 lysozyme refined at 1.7 A resolution. J Mol Biol 193:189-199.
42. Wetlaufer DB. 1973. Nucleation, rapid folding, and globular intrachain regions in proteins. Proc Natl Acad Sci USA 70:697-701.
43. Zehfus MH. 1995. Automatic recognition of hydrophobic clusters and their correlation with protein folding units. Protein Sci 4:1188-1202.
44. Zhang T, Bertelsen E, Benvegnu D, Alber T. 1993. Circular permutation of T4 lysozyme. Biochemistry 32:12311-12318.