Crystallization of a designed peptide from a molten globule ensemble

Folding and Design

Volumn 1, Issue 1, 1996, Pages 57-64

  Betz, Stephen F ^a   Raleigh, Daniel P ^a,c   DeGrado, William F ^a   Lovejoy, Brett ^b,d   Anderson, Daniel ^b   Ogihara, Nancy ^b   Eisenberg, David ^b  

^a DUPONT COMPANY   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

^c STONY BROOK UNIVERSITY   (United States)

^d GLAXOSMITHKLINE   (United States)

Author keywords

Crystallization; Molten globule; Protein design; Protein folding

Indexed keywords

PEPTIDE;

AMINO ACID SEQUENCE; ARTICLE; CHEMICAL STRUCTURE; CHEMISTRY; CIRCULAR DICHROISM; CRYSTALLIZATION; DRUG DESIGN; DRUG STABILITY; ISOLATION AND PURIFICATION; MOLECULAR GENETICS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; SOLUTION AND SOLUBILITY; SPECTROFLUOROMETRY; SYNTHESIS;

AMINO ACID SEQUENCE; CIRCULAR DICHROISM; CRYSTALLIZATION; DRUG DESIGN; DRUG STABILITY; MAGNETIC RESONANCE SPECTROSCOPY; MOLECULAR SEQUENCE DATA; MOLECULAR STRUCTURE; PEPTIDES; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; SOLUTIONS; SPECTROMETRY, FLUORESCENCE;

EID: 0030348047     PISSN: 13590278     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1359-0278(96)00012-0     Document Type: Article

References (40)

1. DeGrado, W.F., Wasserman, Z.R. & Lear, J.D. (1989). Protein design, a minimalist approach. Science 243, 622-628.
2. Bryson, J.W., Betz, S.F., Lu, H.S., Suich, D.J., Zhou, H.X., O'Neil, K.T. & DeGrado, W.F. (1995). Protein design, a hierarchic approach. Science 270, 935-941.
3. Regan, L. & DeGrado, W.F. (1988). Characterization of a helical protein designed from first principles. Science 241, 976-978.
4. Hecht, M.H., Richardson, J.S., Richardson, D.C. & Ogden, R.C. (1990). De novo design, expression and characterization of felix: a four-helix bundle protein of native-like sequence. Science 249, 884-891.
5. Yan, Y. & Erickson, B.W. (1994). Engineering of betabellin 14D: disulfide-induced folding of a β-sheet protein. Protein Sci. 3, 1069-1073.
6. Quinn, T.P., Tweedy, N.B., Williams, R.W., Richardson, J.S. & Richardson, D.C. (1994). Betadoublet: de novo design, synthesis, and characterization of a β-sandwich protein. Proc. Natl. Acad. Sci. U.S.A. 91, 8747-8751.
7. Goraj, K., Renard, A. & Martial, J.A. (1990). Synthesis, purification and initial structure characterization of octarellin, a de novo polypeptide modelled on the alpha/beta barrel proteins. Protein Eng. 3, 259-266.
8. Fedorov, A.N., et al., & Ptitsyn, O.B. (1992). De novo design, synthesis, and study of Albebetin, a polypeptide with a predetermined three-dimensional structure. J. Mol. Biol. 225, 927-931.
9. Tanaka, T., Kimura, H., Hayashi, M., Fujiyoshi, Y., Fukuhara, K.-I. & Nakamura, H. (1994). Characteristics of a de novo designed protein. Protein Sci. 3, 419-427.
10. 8 polypeptides designed for investigating the influence of β-residue packing on the α/β barrel structure stability. Protein Eng. 8, 249-259.
11. Betz, S.F., Raleigh, D.P. & DeGrado, W.F. (1993). De novo protein design: from molten globules to native-like states. Curr. Opin. Struct. Biol. 3, 601-610.
12. Kuwajima, K. (1989). The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure. Proteins 6, 87-103.
13. Ptitsyn, O.B. (1992). The molten globule state. In Protein Folding. (Crieghton, T.E., ed.), pp. 243-299, Freeman, New York.
14. Semisotnov, G.V., Rodionova, N.A., Razgulyaev, O.I., Uversky, V.N., Gripas, A.F. & Gilmanshin, R.I. (1991). Study of the "molten globule" intermediate state in protein folding by a hydrophobic fluorescent probe. Biopolymers 31, 119-128.
15. Haynie, D.T. & Friere, E. (1993). Structural energetics of the molten globule state. Proteins 16, 115-140.
16. Rose, G.D., Gierasch, L.M. & Smith, J.A. (1985). Turns in peptides and proteins. Adv. Protein Chem. 37, 1-109.
17. Eisenberg, D., Wilcox, W., Eshita, S.M., Pryciak, P.M., Ho, S.P. & DeGrado, W.F. (1986). The design, synthesis, and crystallization of an alpha-helical peptide. Proteins 1, 16-22.
18. DeGrado, W.F. (1988). Design of peptides and proteins. Adv. Protein Chem. 39, 51-124.
19. Chakrabartty, A., Kortemme, T. & Baldwin, R.L. (1994). Helix propensities of the amino acids measured in alanine-based peptides without helix-stabilizing side-chain interactions. Protein Sci. 3, 843-852.
20. O'Shea, E.K., Lumb, K.J. & Kim, P.S. (1993). Peptide 'Velcro': design of a heterodimeric coiled coil. Curr. Biol. 3, 658-667.
21. Kuroda, Y., Nakai, T. & Ohkubo, T. (1994). Solution stucture of a de novo helical protein by 2D-NMR spectroscopy. J. Mol. Biol. 236, 862-868.
22. Fezoui, Y., Weaver, D.L. & Osterhout, J.J. (1994). De novo design and structural characterization of an α-helical hairpin peptide: a model system for the study of protein folding intermediates. Proc. Natl. Acad. Sci. U.S.A. 91, 3675-3679.
23. Raleigh, D.P. & DeGrado, W.F. (1992). A de novo designed protein shows a thermally induced transition from a native to a molten globule-like state. J. Am. Chem. Soc. 114, 10079-10081.
24. Raleigh, D.P., Betz, S.F. & DeGrado, W.F. (1995). A de novo designed protein mimics the native state of natural proteins. J. Am. Chem. Soc. 117, 7558-7559.
25. Nautiyal, S., Woolfson, D.N., King, D.S. & Alber, T. (1995). A designed heterotrimeric coiled coil. Biochemistry 34, 11645-11651.
26. 1: implications for protein design. Science 249, 543-546.
27. Lovejoy, B., Choe, S., Cascio, D., McRorie, D.K., DeGrado, W.F. & Eisenberg, D. (1993). Crystal structure of a synthetic triple-stranded alpha-helical bundle. Science 259, 1288-1293.
28. Ho, SP. & DeGrado, W.F. (1987). Design of a 4-helix bundle protein: synthesis of peptides which self-associate into a helical protein. J. Am. Chem. Soc. 109, 6751-6758.
29. Ciesla, D.J., Gilbert, D.E. & Feigon, J. (1991). Secondary structure of the designed peptide alpha-1 determined by nuclear magnetic resonance spectroscopy. J. Am. Chem. Soc. 113, 3957-3961.
30. 1β, a peptide designed to form a four-helix bundle. J. Am. Chem. Soc. 114, 331-337.
31. Prive, G., Ogihara, N., Wesson, L., Cascio, D. & Eisenberg, D. (1995). A designer peptide at high resolution: shake and bake solution of a 400 atom structure. Am. Cryst. Assoc. Ann. Mtg.
32. Ritsyn, O.B. (1987). Protein folding hypotheses and experiments. J. Protein Chem. 6, 273-293.
33. Griko, Y.V., Privalov, P.L., Venyaminov, S.Y. & Kutyshenko, V.P. (1988). Thermodynamic study of the apomyoglobin structure. J. Mol. Biol. 202, 127-138.
34. Ikeguchi, M., Kuwajima, K., Mitani, M. & Sugai, S. (1986). Evidence for identity between the equilibrium unfolding intermediate and a transient folding intermediate: a comparative study of the folding reaction of a-lactalbumin and lysozyme. Biochemistry 25, 6965-6972.
35. Jennings, P.A. & Wright, P.E. (1993). Formation of a molten globule intermediate early in the kinetic pathway of apomyoglobin. Science 262, 892-896.
36. Matthews, B.W. (1968). Solvent content of protein crystals. J. Mol. Biol. 33, 491-497.
37. Cohn, E.J. & Edsall, J.T. (1943) Proteins, amino acids, and peptides as ions and dipolar ions. In Proteins, Amino Acids, and Peptides as Ions and Dipolar Ions, pp. 370-377, Reinhold Publishing Corp, New York.
38. Harding, S.E., Rowe, A.J. & Horton, J.C. (1992) Analytical Ultracentrifugation in Biochemistry and Polymer Science. The Royal Society of Chemistry, Cambridge.
39. Gekko, K. & Hasegawa, Y. (1986). Compressibility-structure relationship of globular proteins. Biochemistry 25, 6563-6571.
40. 2O solutions. Methods Enzymol. 27, 82-98.