Effect of protein fusion on the transition temperature of an environmentally responsive elastin-like polypeptide: A role for surface hydrophobicity?

Protein Engineering, Design and Selection

Volumn 17, Issue 1, 2004, Pages 57-66

  Trabbic Carlson, K ^a   Meyer, D E ^a   Liu, L ^a   Piervincenzi, R ^a   Nath, N ^a   LaBean, T ^a   Chilkoti, A ^b  

^a Duke University   (United States)

^b Duke University   (United States)

Author keywords

Aggregation; Elastin; Fusion protein; Hydrophobicity; Phase transition

Indexed keywords

ELASTIN; GLYCINE; GOLD; HYBRID PROTEIN; PEPTIDE DERIVATIVE; PROLINE; VALINE;

AMINO ACID SEQUENCE; ARTICLE; COLLOID; COMPUTER MODEL; CORRELATION ANALYSIS; HEAT TREATMENT; HYDROPHOBICITY; HYPOTHESIS; LIGAND BINDING; PHASE TRANSITION; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN PURIFICATION; PROTEIN STRUCTURE; PROTEOMICS; TEMPERATURE;

AMINO ACID SEQUENCE; DATABASES; ESCHERICHIA COLI; GOLD COLLOID; LIGANDS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PEPTIDES; PLASMIDS; PROTEIN CONFORMATION; PROTEIN ENGINEERING; PROTEIN FOLDING; RECOMBINANT FUSION PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; SOLUBILITY; SURFACE PLASMON RESONANCE; TEMPERATURE; THERMODYNAMICS;

ESCHERICHIA COLI;

EID: 0842334816     PISSN: 17410126     EISSN: None     Source Type: Journal    
DOI: 10.1093/protein/gzh006     Document Type: Article

References (32)

1. Ausubel, F.M. et al. (1995) Current Protocols in Molecular Biology. John Wiley and Sons, New York.
2. Bain, C.D. et al. (1989) J. Am. Chem. Soc., 111, 321-335.
3. Bundi, A. and Wuthrich, K. (1979) Biopolymers, 18, 285-297.
4. Fauchere, J.L. and Pliska, V. (1983) Eur. J. Med. Chem., 18, 369-375.
5. Kreibig, U. and Vollmer, M. (1995) Optical Properties of Metal Clusters. Springer-Verlag, New York.
6. Lavallie, E.R. et al. (1993) Biotechnology, 11, 187-193.
7. Li, B. and Daggett, V. (2003) Biopolymers, 68, 121-129.
8. Li, B. et al. (2001a) J. Am. Chem. Soc. 123, 11991-11998.
9. Li, B. et al. (2001b) J. Mol. Biol. 305, 581-592.
10. Lovell, S.C. et al. (2003) Proteins: Struct. Func. Genet., 50, 437-450.
11. Luan, C.-H. et al. (1990) Biopolymers, 29, 1699-1706.
12. Luan, C.-H. et al. (1992) Biopolymers, 32, 1251-1261.
13. Matthew, J.B. et al. (1985) CRC Crit. Rev. Biochem., 18, 91-197.
14. Meyer, D.E. and Chilkoti, A (1999) Nat. Biotechnol., 17, 1112-1115.
15. Meyer, D.E. and Chilkoti, A. (2002) Biomacromolecules, 3, 357-367.
16. Meyer, D.E. et al. (2001a) Cancer Res., 61, 1548-1554.
17. Meyer, D.E. et al. (2001b) Biotechnol. Prog., 720-728.
18. Nath, N. and Chilkoti, A. (2001) J. Am. Chem. Soc., 123, 8197-8202.
19. Pattanaik, A. et al. (1991) Biochem. Biophys. Res. Commun., 178, 539-545.
20. Pflugrath, J.W. et al. (1986) J. Mol. Biol. 189, 383-386.
21. Radzicka, A. and Wolfenden, R. (1988) Biochemistry, 27, 1664-1670.
22. Roseman, M.A. (1988) J. Mol. Biol., 200, 513-522.
23. Urry, D.W. (1988) J. Protein Chem., 7, 1-34.
24. Urry, D.W. (1992) Prog. Biophys. Mol. Biol., 57, 23-57.
25. Urry, D.W. (1993) Angew. Chem. Int. Ed. Engl., 32, 819-841.
26. Urry, D.W. (1997) J. Phys. Chem., 101, 11007-11028.
27. Urry, D.W. et al. (1985) Biopolymers, 24, 2345-2356.
28. Urry, D.W. et al. (1991) J. Am. Chem. Soc., 113, 4346-4348.
29. Urry, D.W. et al. (1997) J. Am. Chem. Soc. 119, 1161-1162.
30. Weisbecker, C.S et al. (1996) Langmuir, 12, 3763-3772.
31. Wiegand, G. et al. (1995) J. Mol. Biol., 247, 99-110.
32. Word, J.M. et al. (1999) J. Mol. Biol., 285, 1711-1733.