High helicity of peptide fragments corresponding to β-strand regions of β-lactoglobulin observed by 2D-NMR spectroscopy

Folding and Design

Volumn 1, Issue 4, 1996, Pages 255-263

  Kuroda, Yutaka ^a   Hamada, Daizo ^b   Tanaka, Toshiki ^a   Goto, Yuji ^b  

^a BIOMOL ENG RESEARCH INSTITUTE   (Japan)

^b OSAKA UNIVERSITY   (Japan)

Author keywords

2D NMR; Protein folding; helix; lactoglobulin; strand

Indexed keywords

LACTOGLOBULIN; PEPTIDE FRAGMENT;

AMINO ACID SEQUENCE; ANIMAL; ARTICLE; CATTLE; CHEMISTRY; CIRCULAR DICHROISM; DRUG DESIGN; GENETICS; MOLECULAR GENETICS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; SYNTHESIS;

AMINO ACID SEQUENCE; ANIMALS; CATTLE; CIRCULAR DICHROISM; DRUG DESIGN; LACTOGLOBULINS; MAGNETIC RESONANCE SPECTROSCOPY; MOLECULAR SEQUENCE DATA; PEPTIDE FRAGMENTS; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY;

EID: 0030334664     PISSN: 13590278     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1359-0278(96)00039-9     Document Type: Article

References (46)

1. Collawn, J.F. & Paterson, Y. (1990). Stabilization of helical structure in two 17-residue amphipathic analogues of the C-terminal peptide of cytochrome c. Biopolymers 29, 1289-1296.
2. Dyson, H.J. & Wright, P.E. (1993). Peptide conformation and protein folding. Curr. Opin. Struct. Biol. 3, 60-65.
3. Kuroda, Y. (1993). Residual helical structure in the C-terminal fragment of cytochrome c. Biochemistry 32, 1219-1224.
4. McLeish, M.J., Nielsen, K.J., Wade, J.D. & Craik, D. (1993). A peptide corresponding to the N-terminal 13 residues of T4 lysozyme forms an α-helix. FEBS Lett. 315, 323-328.
5. Oas, T.G. & Kim, P.S. (1988). A peptide model of a protein folding intermediate. Nature 336, 42-48.
6. Waltho, P.J., Feher, V.A, Merutka, G., Dyson, H.J. & Wright, P.E. (1993). Peptide models of protein folding initiation sites. 1. Secondary structure formations by peptides corresponding to the G- and H-helices of myoglobin. Biochemistry 32, 6337-6347.
7. Wu, L.C., Laub, P.B., Elöve, A., Carey, J. & Roder, H. (1993). A noncovalent peptide complex as a model for an early folding intermediate of cytochrome c. Biochemistry 32, 10271-10276.
8. Go, N. (1983). Theoretical studies of protein folding. Annu. Rev. Biophys. Bioeng. 12, 183-210.
9. Kim, P.S. & Baldwin, R.L. (1982). Specific intermediates in the folding reaction of small proteins and the mechanism of protein folding. Annu. Rev. Biochem. 51, 459-489.
10. Baldwin, R.L. (1995). The nature of protein folding pathways: the classical view versus the new view. J. Biomol, NMR 5, 103-109.
11. Hughson, F.M., Wright, P.E. & Baldwin, R.L (1990). Structural characterization of a partly folded state of apomyoglobin. Science 249, 1544-1548.
12. Jeng, M., Englander, S.W., Elöve, G.A., Wand, A.J. & Roder, H. (1990). Structural description of acid-denatured cytochrome c by hydrogen exchange and 2D-NMR. Biochemistry 29, 10433-10437.
13. Kuroda, Y., Endo, S., Nagayama, K. & Wada, A. (1995). Stability of α-helices in the molten globule state of cytochrome c by hydrogen deuterium exchange and two-dimensional NMR spectroscopy. J. Mol. Biol. 247, 682-688.
14. Jennings, P.A. & Wright, P.E. (1993). Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin. Science 262, 892-896.
15. Roder, H., Elöve, G.A. & Englander, S.W. (1988). Structural characterization of folding intermediates in cytochrome c by H-exchange labeling and proton NMR. Nature 335, 700-704.
16. Wright, P.E., Dyson, H.J. & Lerner, R.A. (1988). Conformation of peptide fragments of proteins in aqueous solution: implication for initiation of protein folding. Biochemistry 27, 7167-7175.
17. Papiz, M.Z., et al., & Kraulis, P.J. (1986). The structure of β-lactoglobulin and its similarity to plasma retinol-binding protein. Nature 324, 383-385.
18. Kuwajima, K., Yamaya, H., Miwa, S., Sugai, S. & Nagamura, T. (1987). Rapid formation of secondary structure framework in protein folding studied by stopped flow circular dichroism. FEBS Lett. 221, 115-118.
19. Hamada, D., Segawa, S. & Goto, Y. (1996). Refolding of β-lactoglobulin via α-helical intermediate, submitted.
20. Kuwajima, K. (1996). Stopped-flow circular dichroism. In Circular Dichroism: Conformational Analysis of Biomolecules. (Fasman, G.D., ed.) Plenum, New York, in press.
21. Shiraki, K., Nishikawa, K. & Goto, Y. (1995). Trifluoroethanol stabilization of the α-helical structure of β-lactoglobulin: implication for non-hierarchical protein folding. J. Mol. Biol. 245, 180-194.
22. Dufour, E., Bertrand-Harb, C. & Haertle, T. (1993). Reversible effect of medium dielectric constant on structural transformation of β-lactoglobulin and its retinol binding. Biopolymer 33, 589-598.
23. Hamada, D., Kuroda, Y., Tanaka, T. & Goto, Y. (1995). High helical propensity of the peptide fragments derived from βlactoglobulin, a predominantly β-sheet protein: implication for non-hierarchical protein folding. J. Mol. Biol. 254, 737-740.
24. Nishikawa, K. & Noguchi, T. (1991). Predicting protein secondary structure based on amino acid sequence. Methods Enzymol. 202, 31-44.
25. Dyson, H.J., Merutka, G., Waltho, J.P., Lerner, R.A. & Wright, P.E. (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.
26. Brown, J.E. & Klee, W.A. (1971). Helix-coil transition of the isolated amino terminus of ribonuclease. Biochemistry 10, 470-476.
27. Shoemaker, K.R., Kim, P.S., York, E.J., Stewart, J.M. & Baldwin, R.L. (1987). Tests of the helix dipole model for stabilization of α-helices. Nature 326, 563-567.
28. Blanca, F.J., Rivas, G. & Serrano, L (1994). A short linear peptide that folds into a native stable β-hairpin in aqueous solution. Nat. Struct. Biol. 1, 584-590.
29. Yang, J.J., Pitkeathly, M. & Radford, S.E. (1994). Far-uv circular dichroism reveals a conformational switch in a peptide fragment from the β-sheet of hen lysozyme. Biochemistry 33, 7345-7353.
30. Searle, M., Williams, D.H. & Packman, L.C. (1995). A short linear peptide derived from the N-terminal sequence of ubiquitin folds into a water-stable non-native β-hairpin. Nat. Struct. Biol. 2, 999-1006.
31. Dyson, J., Sayre, J.R., Merutka, G., Shin, H.C., Lerner, R.A. & Wright, P.E. (1992). Folding of peptide fragments comprising the complete sequence of proteins. Models for initiation of protein folding. II. Plastocyanin. J. Mol. Biol. 226, 819-835.
32. Segawa, S., Fukuno, T., Fujiwara, K. & Noda, Y. (1991). Local structures in unfolded lysozyme and correlation with secondary structures in the native conformation: helix forming or breaking propensity of peptide segments. Biopolymers 31, 497-509.
33. Yang, J.J., et al., & Radford, S.E. (1995). Conformational properties of four peptides spanning the sequence of hen lysozyme. J. Mol. Biol. 252, 483-911.
34. Shönnichsen, F.D., Van Eyk, J.E., Hodges, R.S. & Sykes, B.D. (1992). Effect of trifluoroethanol on protein structure. An NMR and CD study using a synthetic actin peptide. Biochemistry 31, 8790-8798.
35. Muñoz, V. & Serrano, L (1994). Elucidating the folding problem of helical peptides in solution. Nat. Struct Biol. 1, 399-409.
36. Wishart, D.S., Sykes, B.D. & Richards, F.M. (1991). Relationship between nuclear magnetic resonance chemical shift and protein secondary structure. J. Mol. Biol. 222, 311-333.
37. Wüthrich, K. (1986). NMR of Proteins and Nucleic Acids. Wiley-Interscience, New York.
38. Kabsch, W. & Sander, C. (1983). Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22, 2577-2637.
39. Rost, B. & Sander, C. (1994). Combining evolutionary information and neural networks to predict protein secondary structure. Proteins 19, 55-72.
40. Rost, B. & Sander, C. (1993). Prediction of protein secondary structure at better than 70% accuracy. J. Mol. Biol. 232, 584-599.
41. Rost, B., Sander, C. & Schneider, R. (1994). PHD-an automatic mail server for protein secondary structure prediction. CABIOS 10, 53-60.
42. Bierzynski, A., Kim, P.S. & Baldwin, R.L. (1982). A salt bridge stabilizes the helix formed by isolated C-peptide of RNase A. Proc. Natl. Acad. Sci. USA 79, 2470-2474.
43. Sancho, J., Neira, J.L. & Fersht, A.R. (1992). An N-terminal fragment of barnase has residual helical structure similar to that in a refolding intermediate. J. Mol. Biol. 224, 749-758.
44. Scholtz, J.M., Qian, H., York, E.J., Stewart, J.M. & Baldwin, R.L. (1991). Parameters of helix-coil transition theory for alanine based peptides of varying chain lengths in water. Biopolymers 31, 1463-1470.
45. Chen, Y.-H., Yang, J.T. & Martinez, H.M. (1972). Determination of the secondary structure of proteins by circular dichroism and optical rotatory dispersion. Biochemistry 11, 4120-4131.
46. Kraulis, P.J. (1991 ). MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24, 946-950.