Hexafluoroacetone hydrate as a structure modifier in proteins: Characterization of a molten globule state of hen egg-white lysozyme

Protein Science

Volumn 6, Issue 5, 1997, Pages 1065-1073

  Bhattacharjya, Surajit ^a   Balaram, Padmanabhan ^a  

^a INDIAN INSTITUTE OF SCIENCE   (India)

Author keywords

CD; fluorescence; hexafluoroacetone; lysozyme; molten globule states; NMR; protein folding

Indexed keywords

ALPHA LACTALBUMIN; EGG WHITE; HEXAFLUOROACETONE; LYSOZYME;

ARTICLE; CARBOXY TERMINAL SEQUENCE; CIRCULAR DICHROISM; FLUORESCENCE; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN FOLDING; PROTEIN TERTIARY STRUCTURE; SITE DIRECTED MUTAGENESIS; STRUCTURE ANALYSIS;

EID: 0030894810     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560060513     Document Type: Article

References (61)

1. Alexandrescu AT, Evans PA, Pitkeathly M, Baum J, Dobson CM. 1993. Structure and dynamics of acid denatured molten globule state of α-lactalbumin: a two-dimensional NMR study. Biochemistry 32:1707-1718.
2. Alexandrescu AT, Ng Y-L, Dobson CM. 1994. Characterization of a trifluoroethanol induced partially folded state of α-lactalbumin. J Mol Biol 235:587-599.
3. Bai Y, Milne JS, Mayne L, Englander SW. 1993. Primary structure effects on peptide group hydrogen exchange. Proteins Struct Fund Genet 17:75-86.
4. Baldwin RL. 1993. Pulsed H/D exchange studies of folding intermediates. Curr Opin Struct Biol 3:84-91.
5. Baum J, Dobson CM, Evans PA, Hanley C. 1989. Characterization of a partly folded protein by NMR methods: Studies on the molten globule state of guinea pig α-lactalbumin. Biochemistry 28:7-13.
6. Blake CCF, Koening DF, Mair GA, North ACT, Phillips DC, San VR. 1965. Structure of hen egg white lysozyme. Nature (London) 206:757-761.
7. Bolin KA, Pitkeathly M, Miranker A, Smith LJ, Dobson CM. 1996. Insight into a random coil conformation and an isolated helix: Structured and dynamical characterization of the c-helix peptide from hen lysozyme. J Mol Biol 261:443-453.
8. Bruch MD, Dhingra MM, Gierasch LM. 1992. Side-chain backbone hydrogen bonding contribution to helix stability in peptides derived from an a-helical region of carboxypeptidase A. Proteins Struct Funct Genet 10:130-139.
9. Buck M, Radford SE, Dobson CM. 1993. A partially folded state of hen egg white lysozyme in trifluoroethanol: Structural characterization and implication for protein folding. Biochemistry 32:669-678.
10. Buck M, Schwalbe H, Dobson CM. 1995. Characterization of conformational preferences in a partly folded protein by heteronuclear NMR spectroscopy: Assignment and secondary structure analysis of hen egg-white lysozyme in trifluoroethanol. Biochemistry 34:13219-13232.
11. 15N NMR relaxation measurements of hen egg white lysozyme denatured in trifluoroethanol. J Mol Biol 257:669-683.
12. Bychkova VE, Berni R, Rossi G-L, Kutyshenko VP, Ptitsyn OB. 1992. Retinol-binding protein is in the molten globule state at low pH. Biochemistry 31:7566-7511.
13. Bychkova VE, Dujsekina AE, Klenin SI, Tiktopulo EI, Uversky VN, Ptitsyn OB. 1996. Molten globule-like state of cytochrome c under conditions simulating those near the member surface. Biochemistry 35:6058-6063.
14. Carra JH, Anderson EA, Privalov PL. 1994. Thermodynamics of the staphylococcal nuclease denaturation. II. The A-state. Protein Science 3:952-959.
15. Chakrabartty A, Schellman JA, Baldwin RL. 1991. Large difference in the helix propensities of alanine and glycine. Nature (London) 351:586-588.
16. Chakrabartty A, Kortemme T, Padmanabhan S, Baldwin RL. 1993. Aromatic side-chain contribution to far-ultraviolet circular dichroism of helical peptides and its effect on measurement of helix propensities. Biochemistry 32:5560-5565.
17. Chen X, Rambo R, Matthews CR. 1992. Amino acid replacements can selectively affect the interaction energy of autonomous folding units in the α subunit of tryptophan synthase. Biochemistry 31:2219-2223.
18. Chyan C-L, Wormald C, Dobson CM, Evans PA, Baum J. 1993. Structure and stability of the molten globule state of guinea-pig α-lactalbumin: A hydrogen exchange study. Biochemistry 32:5681-5691.
19. Dobson CM. 1992. Unfolded proteins, compact states and molten globules. Curr Opin Struct Biol 2:6-12.
20. Dobson CM, Evans PA. 1984. Protein folding kinetics from magnetization transfer nuclear magnetic resonance. Biochemistry 23:4267-4270.
21. Dyson HJ, Merutka G, Waltho JP, Lerner RA, Wright PE. 1992. Folding of peptide fragments comprising the complete sequence of proteins. Models for initiation of protein folding. I. Myohemerythrin. J Mol Biol 226:795-817.
22. Englander SW, Kallenbach NR. 1984. Hydrogen exchange and structural dynamics of proteins and nucleic acids. Q Rev Biophys 16:521-655.
23. Fan P, Bracken C, Baum J. 1993. Structural characterization of monellin in the alcohol-denatured state by NMR: Evidence for β-sheet to α-helix conversion. Biochemistry 32:1573-1582.
24. Freire E. 1995. Thermodynamics of partly folded intermediates in proteins. Annu Rev Biophys Biomol Struct 24:1-16.
25. Goodman M, Rosen GI. 1964. Conformational aspects of polypeptide structure XVI. Rotatory constants, cotton effects, and ultraviolet absorption data for glutamate oligomers and co-oligomers. Biopolymers 2:537-559.
26. Goodwin CA, Allen TJ, Oslick SL, McClure KF, Lee JH, Kemp DS. 1996. Mechanism of stabilization of helical conformations of polypeptides by water containing trifluoroethanol. J Am Chem Soc 118:3082-3090.
27. Harding MM, Williams DH, Woolfson DN. 1991. Characterization of a partially denatured state of a protein by two-dimensional NMR: Reduction of the hydrophobic interactions in ubiqutin. Biochemistry 30:3120-3128.
28. Hughson FM, Barrick D, Baldwin RL. 1991. Probing the stability of a partly folded apomyoglobin intermediate by site-directed mutagenesis. Biochemistry 30:4113-4118.
29. Hughson FM, Wright PE, Baldwin RL. 1992. Structural characterization of a partly folded apomyoglobin intermediate. Science 249:1544-1548.
30. Itzhaki LS, Evans PA, Dobson CM, Radford SE. 1994. Tertiary interaction in the folding pathway of hen lysozyme: Kinetic studies using fluorescent probes. Biochemistry 33:5212-5220.
31. Jeng MF, Englander SW, Elove GA, Wand AJ, Roder H. 1990. Structural description of acid-denatured cytochrome c by hydrogen exchange and 2-D NMR. Biochemistry 29:10433-10437.
32. Kamatari YO, Konno T, Kataoka M, Akasaka K. 1996. The methanol-induced globular and expanded denatured states of cytochrome c: A study by CD, fluorescence, NMR and small angle X-ray scattering. J Mol Biol 259:512-523.
33. Kuroda Y, Kidokoro S, Wada A. 1992. Thermodynamic characterization of cytochrome c at low pH, observation of the molten globule state and of the cold denaturation process. J Mol Biol 223:1139-1153.
34. Kuwajima K. 1989. The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure. Proteins Struct Funct Genet 6:87-103.
35. Lala AK, Kaul P. 1992. Increased exposure of hydrophobic surface in molten globule state of α-lactalbumin. J Biol Chem 28:19914-19918.
36. Lehrer SS. 1971. Solute perturbation of protein fluorescence. The quenching of the tryptophyl fluorescence of the model compounds and of lysozyme by iodide ion. Biochemistry 10:3254-3263.
37. Lin L, Pinker RJ, Rose GD, Kallenbach, NR. 1994. Molten globule characteristics of the native state of apomyoglobin. Nature Struct Biol 1:447-451.
38. Longworth R. 1964. Fluoroketone hydrates: Helix-breaking solvents for polypeptides and proteins. Nature 203:295-296.
39. Molday RS, Englander SW, Kallen RG. 1972. Primary structure effects on peptide groups hydrogen exchange. Biochemistry 11:150-158.
40. Morozova LA, Haynie DT, Arico-Muende C, Deal HV, Dobson CM. 1995. Structural basis of the stability of a molten globule. Nature Struct Biol 2:871-875.
41. Murto J, Kivinen A, Lundstrom G. 1971. Fluoroalcohols, Part 14. Densities, refractive indices, viscosities, and isothermal vapour-liquid equilibria of hexafluoroacetone-water mixture. Acta Chem Scand 25:2451-2456.
42. Nelson JW, Kallenbach NR. 1989. Persistence of the α-helix stop signal in the S-peptide in trifluoroethanol solutions. Biochemistry 28:5256-5261.
43. Nishii I, Kataoka M, Tokunaga F, Goto Y. 1994. Cold denaturation of the molten globule states of apomyoglobin and a profile for protein folding. Biochemistry 33:4903-4909.
44. O'Neil KT, Degrado WF. 1990. A thermodynamic scale for the helix-forming tendencies of the commonly occurring aminoacids. Science 250:646-650.
45. Peng Z, Kim PS. 1994. A protein dissection study of a molten globule. Biochemistry 33:2136-2141.
46. Privalov PL. 1992. Physical basis of the stability of the folded conformations of proteins. In: Creighton TE, ed., Protein Folding. New York: W.H. Freeman and Company, pp 83-125.
47. Ptitsyn OG. 1992. The molten globule state. In: Creighton TE, ed., Protein Folding. New York: W.H. Freeman and Company, pp 243-300.
48. Ptitsyn OG. 1995. Structures of folding intermediates. Curr Opin Struct Biol 5:74-78.
49. Radford SE, Buck M, Topping KD, Dobson CM, Evans PA. 1992a. Hydrogen exchange in native and denatured states of hen egg-white lysozyme. Proteins Struct Fund Genet 14:23-248.
50. Radford SE, Dobson CM. 1995. Insight into protein folding using physical techniques: Studies of lysozyme and α-lactalbumin. Phil Trans R Soc Lond B384:17-25.
51. Radford SE, Dobson CM, Evans PA. 1992b. The folding of hen lysozyme involves partially structured intermediates and multiple pathways. Nature (London) 358:302-307.
52. Rajan R, Awasthi SK, Bhattachrjya S, Balaram P. 1997. Teflon coated peptides: Hexafluoroacetone trihydrate as a structure stabilizer for peptides. Biopolymers. In press.
53. Rajan R, Balaram P. 1996. A model for the interaction of trifluoroethanol with peptides and proteins. Int J Peptides Protein Res 48:328-336.
54. 1H NMR assignment and secondary structure of hen egg white lysozyme in solution. Biochemistry 27:122-136.
55. Redfield C, Smith RAG, Dobson CM. 1994. Structural characterization of a highly-ordered "molten globule" at low pH. Nature Struct Biol 1:23-29.
56. Sanz JM, Fersht AR. 1993. Rationally designing the accumulation of a folding intermediate of barnase by protein engineering. Biochemistry 32:13584-13592.
57. Schulman BA, Redfield C, Peng Z-Y, Dobson CM, Kim PS. 1995. Different subdomains are most protected from hydrogen exchange in the molten globule and native states of human α-lactalbumin. J Mol Biol 253:651-657.
58. Shiraki K, Nishikawa K, Goto Y. 1995. Trifluoroethanol-induced stabilization of the α-helical structure of β-lactoglobulin: implication for non-hierarchical protein folding. J Mol Biol 245:180-194.
59. Shortle D. 1996. The denatured state (the other half of the folding equation) and its role in protein stability. FASEB 10:27-34.
60. Sonnichsen FD, Van Eyk JE, Hodges RS, Sykes BD. 1992. Effect of trifluoroethanol on protein structure: An NMR and CD study using a synthetic actin peptide. Biochemistry 31:8790-8798.
61. Vuilleumier S, Sancho J, Loewenthal R, Fersht AR. 1993. Circular dichroism studies of bamase and its mutants: Characterization of the contribution of aromatic side chains. Biochemistry 32:10303-10313.