Stabilization of proteins by rational design of α-helix stability using helix/coil transition theory

Folding and Design

Volumn 1, Issue 1, 1996, Pages 29-34

  Villegas, Virtudes ^a   Viguera, Ana Rosa ^b   Avilés, F Xavier ^a   Serrano, Luis ^b  

^a UNIVERSITAT AUTÒNOMA DE BARCELONA   (Spain)

^b EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

Author keywords

Helix prediction; Helix stability; Mutants; NMR; Protein stability

Indexed keywords

CARBOXYPEPTIDASE; CARBOXYPEPTIDASE A; ENZYME PRECURSOR; PEPTIDE; PEPTIDE FRAGMENT; PROTEIN;

ALGORITHM; AMINO ACID SEQUENCE; ARTICLE; CHEMICAL MODEL; CHEMISTRY; CIRCULAR DICHROISM; DRUG DESIGN; DRUG STABILITY; GENETICS; HUMAN; IN VITRO STUDY; MOLECULAR GENETICS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN ENGINEERING; PROTEIN SECONDARY STRUCTURE; SITE DIRECTED MUTAGENESIS; SYNTHESIS; THERMODYNAMICS;

ALGORITHMS; AMINO ACID SEQUENCE; CARBOXYPEPTIDASES; CARBOXYPEPTIDASES A; CIRCULAR DICHROISM; DRUG DESIGN; DRUG STABILITY; ENZYME PRECURSORS; HUMANS; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, CHEMICAL; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PEPTIDE FRAGMENTS; PEPTIDES; PROTEIN ENGINEERING; PROTEIN STRUCTURE, SECONDARY; PROTEINS; THERMODYNAMICS;

EID: 0030334742     PISSN: 13590278     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1359-0278(96)00009-0     Document Type: Article

References (32)

1. Adams, M.W.W. & Kelly, R.M., eds (1992). Biocatalysis at extreme temperatures: enzyme systems near and above 100°C. ACS press, Washington.
2. Serrano, L., Tony, T. & Fersht, A.R. (1993). The step-wise mutation of barnase to binase and a procedure for engineering increased stability of proteins: an experimental analysis of the evolution of protein stability. J. Mot. Biol. 233, 305-312.
3. Lee, C. & Levitt, M. (1991). Accurate prediction of the stability and activity effects of site-directed mutagenesis on a protein core. Nature 352, 448-451.
4. Simonson, T. & Brunger, A.T. (1992). Thermodynamics of protein-peptide interactions in the ribonuclease S-system studied by molecular dynamics and free energy calculation. Biochemistry 31, 8661-8674.
5. Van Gunsteren, W.F. & Mark, A.E (1992). Prediction of the activity and stability effects of site-directed mutagenesis on a protein core. J. Mol. Biol. 227, 389-395.
6. Pickett, S.D. & Sternberg, M.J.E. (1993). Empirical scale of side-chain conformational entropy in protein folding. J. Mol. Biol. 231, 825-839.
7. Totrov, M.M. & Abagyan, R.A. (1992). Detailed ab initio prediction of lysozyme-antibody complex with 1.6 Å accuracy. Nature Struct. Biol. 1, 259-265.
8. De Filippis, V., Sander, C. & Vriend, G. (1994). Predicting local structural changes that result from point mutations. Prot. Eng. 7, 1203-1208.
9. Lee, C. (1994). Predicting protein mutant energetics by self-consistent ensemble optimization. J. Mol. Biol. 236, 918-939.
10. Pielak, G.J., et al. & Trojak, S.K. (1995). Protein thermal denaturation. Side-chain models and evolution: amino acid substitutions at a conserved helix-helix interface. Biochemistry 34, 3268-3276.
11. Chakrabartty, A. & Baldwin, R.L. (1995). Stability of α-helices. Adv. Prot. Chem. 46, 141-176.
12. Serrano, L. & Fersht, A.R. (1989). Capping and α-helix stability. Nature 342, 296-299.
13. Nicholson, H., Anderson, D.E., Dao-Pin, S. & Matthews, B.W. (1991). Analysis of the interaction between charged side chains and the α-helix dipole using designed thermostable mutants of phage T4 lysozyme. Biochemistry 30, 9816-9828.
14. Horovitz, A., Matthews, J. & Fersht, A.R. (1992). α-Helix stability in proteins. II. Factors that influence stability at an internal position. J. Mol. Biol. 227, 560-568.
15. Serrano, L., Sancho, J., Hirshberg, J.M. & Fersht, A.R. (1992). α-Helix stability in proteins. I. Empirical correlations concerning substitution of side chains at the N- and C-caps and the replacement of alanine by glycine or serine at solvent-exposed surfaces. J. Mol. Biol. 227, 544-549.
16. as and protein stability. Biochemistry 31, 2253-2258.
17. Blaber, M., Zang, X. & Matthews, B. (1993). Structural basis of amino acid α-helix propensity. Science 260, 1637-1640.
18. Muñoz, V. & Serrano, L (1995). Elucidating the folding problem of helical peptides using empirical parameters, II: helix macrodipole effects and rational modification of the helical content of natural peptides. J. Mol. Biol. 245, 275-296.
19. Muñoz, V. & Serrano, L (1995). Elucidating the folding problem of helical peptides using empirical parameters. III: Temperature and pH dependence. J. Mol. Biol. 245, 297-308.
20. Vendrell J., Billeter M., Wider G., Avilés, F.X. & Wüthrich, K. (1991). Three-dimensional structure of porcine procarboxypeptidase B: a structural basis of its inactivity. EMBO J. 10, 11-15.
21. Coll M., Guasch, A., Avilés, F.X. & Huber, R. (1991). The NMR structure of the activation domain isolated from procarboxypeptidase B. EMBO J. 10, 1-9.
22. Guasch, A., Coll, M., Avilés, F.X. & Huber, R. (1992). Three dimensional structure of porcine pancreatic procarboxypeptidase A. A comparison of the A and B zymogens and their determinants for inhibition and activation. J. Mol. Biol. 224, 141-157.
23. Catasús, LI, Vendrell, J., Avilés, F.X., Carreira, S., Puigserver, A., & Billeter, M. (1995). The sequence and conformation of human pancreatic procarboxypeptidase A2. cDNA cloning, sequence analysis and 3D model. J. Biol. Chem. 270, 6651-6657.
24. Villegas, V., Azuaga, A., Catasus, LI., Reverter, D., Mateo, P.L., Aviles, F.X. & Serrano, L (1995). Evidence for a two-state transition in the folding process of the activation domain of human procarboxypeptidase A2. Biochemistry in press.
25. Sanchez-Ruiz, J.M., Lopez-Lacomba, J.L, Mateo, P.L., Vilanova, M., Serra, M.A. & Avilés, F.X. (1988). Analysis of the thermal unfolding of porcine procarboxypeptidase A and its functional process by DSC. Eur. J. Biochem. 176, 225-230.
26. Conejero-Lara, F., Sanchez-Ruiz, J.M., Mateo, P.L., Burgos, F.J., Vendrell, J. & Avilés, F.X. (1991). DSC study of carboxypeptidase B, procarboxypeptidase B and its activation domain. Eur. J. Biochem. 200, 663-670.
27. Chen, Y.H., Yang, J.T. & Chau, K.H. (1974). Determination of the helix and β-form of proteins in aqueous solution by circular dichroism. Biochemistry 13, 3350-3359.
28. Johnson, C.M. & Fersht, A.R. (1995). Protein stability as a function of denaturant concentration: the thermal stability of barnase in the presence of urea. Biochemistry 34, 6795-6804.
29. Gill, S.C. & Von Hippel, P.H. (1989). Calculation of protein extinction coefficients from amino acid sequence data. Anal. Biochem. 182, 319-326.
30. Wüthrich, K. (1986). NMR of Proteins and Nucleic Acids. John Wiley & Sons. New York.
31. Kabsch, W. & Sander, C. (1983). Dictionary of protein secondary structure. Biopolymers 20, 1080-1085.
32. 1H chemical shifts obtained as a function of temperature and trifluoroethanol concentration for the peptide series GGXGG. J. Biomol. NMR 5, 14-24.