Dynamics of a partially stretched protein molecule studied using an atomic force microscope

Biophysical Chemistry

Volumn 107, Issue 1, 2004, Pages 51-61

  Okajima, Takaharu ^a,b   Arakawa, Hideo ^a   Taufiq Alam, Mohammad ^a   Sekiguchi, Hiroshi ^a   Ikai, Atsushi ^a  

^a TOKYO INSTITUTE OF TECHNOLOGY   (Japan)

^b HOKKAIDO UNIVERSITY   (Japan)

Author keywords

Atomic force microscope; Carbonic anhydrase; Dynamics; Force spectroscopy; Mechanical unfolding; Viscoelasticity

Indexed keywords

CARBONATE DEHYDRATASE II; GLOBULAR PROTEIN; MONOMER;

ARTICLE; ATOMIC FORCE MICROSCOPY; CONTROLLED STUDY; CORRELATION ANALYSIS; ENZYME ACTIVITY; GENETIC ENGINEERING; MEASUREMENT; MOLECULAR DYNAMICS; MOLECULAR INTERACTION; MOLECULAR MECHANICS; NONHUMAN; OSCILLATION; PHASE TRANSITION; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN INTERACTION; PROTEIN TARGETING; TENSILE STRENGTH;

BOVINAE; ESCHERICHIA COLI;

EID: 1042267431     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bpc.2003.08.006     Document Type: Article

References (27)

1. Binnig G., Quate C.F., Gerber Ch. Atomic force microscope. Phys. Rev. Lett. 56:1986;930-933.
2. Rief M., Gautel M., Oesterhelt F., Fernandez J.M., Gaub H.E. Reversible unfolding of individual titin immunoglobulin domains by AFM. Science. 276:1997;1109-1112.
3. Mitsui K., Hara M., Ikai A. Mechanical unfolding of alpha-2- macroglobulin with atomic force microscope. FEBS Lett. 385:1996;29-33.
4. Ikai A., Mitsui K., Furutani Y., Hara M., McMurty J., Wong K.P. Protein stretching II: results for carbonic anhydrase. Jpn. J. Appl. Phys. 36:1997;3887-3893.
5. Ikai A., Wang T. Protein stretching IV. Analysis of the force-extension curves. Jpn. J. Appl. Phys. 39:2000;3784-3788.
6. Carrion-Vazquez M., Oberhauser A.F., Fowler S.B., Marszalek P.E., Broedel S.E., Clarke J., et al. Mechanical and chemical unfolding of a single protein: a comparison. Proc. Natl. Acad. Sci. USA. 96:1999;3694-3699.
7. Idris A., Alam M.T., Ikai A. Spring mechanics of alpha-helical polypeptide. Protein Eng. 13:2000;763-770.
8. Oesterhelt F., Oesterhelt D., Pfeiffer M., Engel A., Gaub H.E., Müller D.J. Unfolding pathways of individual bacteriorhodopsins. Science. 288:2000;143-146.
9. Oberhauser A.F., Marszalek P.E., Erickson H.P., Fernandez J.M. The molecular elasticity of the extracellular matrix protein tenascin. Nature. 393:1998;181-185.
10. Oberhauser A.F., Hansma P.K., Carrion-Vazquez M., Fernandez J.M. Stepwise unfolding of titin under force-clamp atomic force microscopy. Proc. Natl. Acad. Sci. USA. 98:2001;468-472.
11. Rief M., Clausen-Schaumann H., Gaub H.E. Sequence-dependent mechanics of single DNA molecules. Nat. Struct. Biol. 6:1999;346-349.
12. Mitsui K., Nakajima K., Arakawa H., Hara M., Ikai A. Dynamic measurement of single protein's mechanical properties. Biochem. Biophys. Res. Commun. 272:2000;55-63.
13. Kageshima M., Lantz M.A., Jarvis S.P., Tokumoto H., Takeda S., Ptak A., et al. Insight into conformational changes of a single alpha-helix peptide molecule through stiffness measurements. Chem. Phys. Lett. 343:2001;77-82.
14. Sakai Y., Ikehara T., Nishi T., Nakajima K., Hara M. Nanorheology measurement on a single polymer chain. Appl. Phys. Lett. 81:2002;724-726.
15. Humphris A.D.L., Miles M.J. Atomic force microscopy in cell biology. Jena B.P., Heinrich Hörber J.K. in Methods in Cell Biology, Vol. 68. 2002;337 Academic Press, San Diego.
16. Radmacher M., Tillmann R.W., Fritz M., Gaub H.E. From molecules to cells: imaging soft samples with the atomic force microscope. Science. 257:1992;1900-1905.
17. Radmacher M., Tillmann R.W., Gaub H.E. Imaging viscoelasticity by force modulation with the atomic force microscope. Biophys. J. 64:1993;735-742.
18. Magnov S.N., Elings V., Whangbo M.-H. Phase imaging and stiffness in tapping-mode atomic force microscopy. Surf. Sci. 375:1997;L385-L391.
19. Alam M.T., Ikai A. Protein stretching V: two forms of carbonic dehydratase detected by force microscopy. Appl. Phys. A. 72:2001;S121-S124.
20. Alam M.T., Yamada T., Carlsson U., Ikai A. The importance of being knotted: effects of the C-terminal knot structure on enzymatic and mechanical properties of bovine carbonic anhydrase II. FEBS Lett. 519:2002;35-40.
21. R. Saito, Master's Thesis, Tokyo Institute of Technology, 2002.
22. Hutter J.L., Bechhoefer J. Calibration of atomic-force microscope tips. Rev. Sci. Instrum. 64:1993;1868-1873.
23. Sekiguchi H., Arakawa H., Okajima T., Ikai A. Non-destructive force measurement in liquid using atomic force microscope. Appl. Surf. Sci. 188:2002;489-492.
24. Semisotnov G.V., Rodionova N.A., Kutyshenko V.P., Ebert B., Blanck J., Ptitsyn O.B. Sequential mechanism of refolding of carbonic anhydrase B. FEBS Lett. 224:1987;9-13.
25. Freskgård P.-O., Carlsson U., Mårtensson L.-G., Jonsson B.-H. Folding around the C-terminus of human carbonic anhydrase II. FEBS Lett. 289:1991;117-122.
26. Svensson M., Jonasson P., Freskgård P.-O., Jonsson B.-H., Lindgren M., Mårtensson L.G., et al. Mapping the folding intermediate of human carbonic anhydrase II. Probing substructure by chemical reactivity and spin and fluorescence labeling of engineered cysteine residues. Biochemistry. 34:1995;8606-8620.
27. Lavecchia R., Zugaro M. Thermal denaturation of erythrocyte carbonic anhydrase. FEBS Lett. 292:1991;162-164.