Biophysical investigations of engineered polyproteins: Implications for force data

Biophysical Journal

Volumn 88, Issue 3, 2005, Pages 2022-2029

  Rounsevell, Ross W S ^a   Steward, Annette ^a   Clarke, Jane ^a  

^a UNIVERSITY OF CAMBRIDGE   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

FIBRONECTIN; MONOMER; MUTANT PROTEIN; POLYPROTEIN; SODIUM CHLORIDE; TENASCIN; PEPTIDE FRAGMENT; RECOMBINANT PROTEIN; TENASCIN FIBRONECTIN TYPE III DOMAIN (1 92); TENASCIN FIBRONECTIN TYPE III DOMAIN (1-92);

ARTICLE; CALCULATION; DYNAMIC FORCE MICROSCOPY; ELECTRIC POTENTIAL; FORCE; INDUCED MUTATION; KINETICS; MICROSCOPY; MOLECULAR CLONING; MOLECULAR INTERACTION; MUTATIONAL ANALYSIS; PH; PHYSICAL CHEMISTRY; PROTEIN ANALYSIS; PROTEIN DOMAIN; PROTEIN ENGINEERING; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION; PROTEIN STABILITY; SALINITY; TANDEM REPEAT; TECHNIQUE; THERMODYNAMICS; ATOMIC FORCE MICROSCOPY; BIOPHYSICS; CHEMISTRY; ELASTICITY; GENETICS; HUMAN; MACROMOLECULE; MECHANICAL STRESS; METHODOLOGY; MICROMANIPULATION; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN TERTIARY STRUCTURE; ULTRASTRUCTURE;

BIOPHYSICS; ELASTICITY; HUMANS; HYDROGEN-ION CONCENTRATION; KINETICS; MACROMOLECULAR SUBSTANCES; MICROMANIPULATION; MICROSCOPY, ATOMIC FORCE; PEPTIDE FRAGMENTS; POLYPROTEINS; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN ENGINEERING; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT PROTEINS; STRESS, MECHANICAL; TENASCIN;

EID: 20544435808     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.104.053744     Document Type: Article

References (33)

1. Akke, M., J. Liu, J. Cavanagh, H. P. Erickson, and A. G. Palmer. 1998. Pervasive conformational fluctuations on microsecond time scales in a fibronectin type III domain. Nat. Struct. Biol. 5:55-59.
2. Best, R. B., S. B. Fowler, J. L. Toca-Herrera, and J. Clarke. 2002. A simple method for probing the mechanical unfolding pathway of proteins by protein engineering phi-value analysis. Proc. Natl. Acad. Sci. USA. 99: 12143-12148.
3. Best, R. B., S. B. Fowler, J. L. Toca-Herrera, A. Steward, E. Paci, and J. Clarke. 2003. Mechanical unfolding of a titin Ig domain: structure of transition state revealed by combining atomic force microscopy, protein engineering and molecular dynamics simulations. J. Mol. Biol. 330:867-877.
4. Best, R. B., H. B. Li, A. Steward, V. Daggett, and J. Clarke. 2001. Can non-mechanical proteins withstand force? Stretching barnase by atomic force microscopy and molecular dynamics simulation. Biophys. J. 81:2344-2356.
5. Brockwell, D. J., E. Paci, R. C. Zinober, G. S. Beddard, P. D. Olmsted, D. A. Smith, R. N. Perham, and S. E. Radford. 2003. Pulling geometry defines the mechanical resistance of a β-sheet protein. Nat. Struct. Biol. 10:731-737.
6. Carr, P. A., H. P. Erickson, and A. G. Palmer. 1997. Backbone dynamics of homologous fibronectin type III cell adhesion domains from fibronectin and tenascin. Structure. 5:949-959.
7. Carrion-Vazquez, M., H. B. Li, H. Lu, P. E. Marszalek, A. F. Oberhauser, and J. M. Fernandez. 2003. The mechanical stability of ubiquitin is linkage dependent. Nat. Struct. Biol. 10:738-743.
8. Carrion-Vazquez, M., A. F. Oberhauser, S. B. Fowler, P. E. Marszalek, S. E. Broedel, J. Clarke, and J. M. Fernandez. 1999. Mechanical and chemical unfolding of a single protein: a comparison. Proc. Natl. Acad. Sci. USA. 96:3694-3699.
9. Clarke, J., S. J. Hamill, and C. M. Johnson. 1997. Folding and stability of a fibronectin type III domain of human tenascin. J. Mol. Biol. 270:771-778.
10. Cota, E., S. J. Hamill, S. B. Fowler, and J. Clarke. 2000. Two proteins with the same structure respond very differently to mutation-the role of plasticity in protein stability. J. Mol. Biol. 302:713-725.
11. Fersht, A. R., A. Matouschek, and L. Serrano. 1992. The folding of an enzyme. I. Theory of protein engineering analysis of stability and pathway of protein folding. J. Mol. Biol. 224:771-782.
12. Fowler, S. B., and J. Clarke. 2001. Mapping the folding pathway of an immunoglobulin domain: structural detail from phi-value analysis and movement of the transition state. Structure. 9:355-366.
13. Hamill, S. J., A. E. Meekhof, and J. Clarke. 1998. The effect of boundary selection on the stability and folding of the third fibronectin type III domain from human tenascin. Biochemistry. 37:8071-8079.
14. Hamill, S. J., A. Steward, and J. Clarke. 2000. The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J. Mol. Biol. 297:165-178.
15. Kellermayer, M. S. Z., S. B. Smith, H. L. Granzier, and C. Bustamante. 1997. Folding-unfolding transitions in single titin molecules characterized with laser tweezers. Science. 276:1112-1116.
16. Kraulis, P. 1991. MolScript, a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24:946-950.
17. Law, R., P. Carl, S. Harper, P. Dalhaimer, D. W. Speicher, and D. E. Discher. 2003a. Cooperativity in forced unfolding of tandem spectrin repeats. Biophys. J. 84:533-544.
18. Law, R., G. Liao, S. Harper, G. L. Yang, D. W. Speicher, and D. E. Discher. 2003b. Pathway shifts and the thermal softening in temperature-coupled forced unfolding of spectrin domains. Biophys. J. 85:3286-3293.
19. Leahy, D. J., W. A. Hendrickson, I. Aukhil, and H. P. Erickson. 1992. Structure of a fibronectin type III domain from tenascin phased by MAD analysis of the selenomethionyl protein. Science. 258:987-991.
20. Lenne, P. F., A. J. Raae, S. M. Altmann, M. Saraste, and J. K. H. Horber. 2000. States and transitions during forced unfolding of a single spectrin repeat. FEBS Lett. 476:124-128.
21. Li, H. B., M. Carrion-Vazquez, A. F. Oberhauser, P. E. Marszalek, and J. M. Fernandez. 2000a. Point mutations alter the mechanical stability of immunoglobulin modules. Nat. Struct. Biol. 7:1117-1120.
22. Li, H. B., A. F. Oberhauser, S. B. Fowler, J. Clarke, and J. M. Fernandez. 2000b. Atomic force microscopy reveals the mechanical design of a modular protein. Proc. Natl. Acad. Sci. USA. 92:6527-6531.
23. Lightner, V. A., and H. P. Erickson. 1990. Binding of hexabrachion (tenascin) to the extracellular matrix and substratum and its effect on cell adhesion. J. Cell Sci. 95:263-277.
24. MacDonald, R. I., and E. V. Pozharski. 2001. Free energies of urea and of thermal unfolding show that two tandem repeats of spectrin are thermodynamically more stable than a single repeat. Biochemistry. 40:3974-3984.
25. Meekhof, A. E., S. J. Hamill, V. L. Arcus, J. Clarke, and S. M. V. Freund. 1998. The dependence of chemical exchange on boundary selection in a fibronectin type III domain from human tenascin. J. Mol. Biol. 282: 181-194.
26. Oberhauser, A. F., P. E. Marszalek, H. P. Erickson, and J. M. Fernandez. 1998. The molecular elasticity of the extracellular matrix protein tenascin. Nature. 393:181-185.
27. Rief, M., M. Gautel, F. Oesterhelt, J. M. Fernandez, and H. E. Gaub. 1997. Reversible unfolding of individual titin immunoglobulin domains by AFM. Science. 276:1109-1112.
28. Rief, M., J. Pascual, M. Saraste, and H. E. Gaub. 1999. Single molecule force spectroscopy of spectrin repeats: low unfolding forces in helix bundles. J. Mol. Biol. 286:553-561.
29. Scott, K. A., A. Steward, S. B. Fowler, and J. Clarke. 2002. Titin; a multidomain protein that behaves as the sum of its parts. J. Mol. Biol. 315:819-829.
30. Steward, A., J. L. Toca-Herrera, and J. Clarke. 2002. Versatile cloning system for construction of multimeric proteins for use in atomic force microscopy. Protein Sci. 11:2179-2183.
31. Tskhovrebova, L., J. Trinick, J. A. Sleep, and R. M. Simmons. 1997. Elasticity and unfolding of single molecules of the giant muscle protein titin. Nature. 387:308-312.
32. Williams, P. M., S. B. Fowler, R. B. Best, J. L. Toca-Herrera, K. A. Scott, A. Steward, and J. Clarke. 2003. Hidden complexity in the mechanical properties of titin. Nature. 422:446-449.
33. Wright, C. F., K. Lindorff-Larsen, L. G. Randles, and J. Clarke. 2003. Parallel protein-unfolding pathways revealed and mapped. Nat. Struct. Biol. 10:658-662.