Literature DB >> 10500301

The study of protein mechanics with the atomic force microscope.

T E Fisher1, A F Oberhauser, M Carrion-Vazquez, P E Marszalek, J M Fernandez.   

Abstract

The unfolding and folding of single protein molecules can be studied with an atomic force microscope (AFM). Many proteins with mechanical functions contain multiple, individually folded domains with similar structures. Protein engineering techniques have enabled the construction and expression of recombinant proteins that contain multiple copies of identical domains. Thus, the AFM in combination with protein engineering has enabled the kinetic analysis of the force-induced unfolding and refolding of individual domains as well as the study of the determinants of mechanical stability.

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Year:  1999        PMID: 10500301     DOI: 10.1016/s0968-0004(99)01453-x

Source DB:  PubMed          Journal:  Trends Biochem Sci        ISSN: 0968-0004            Impact factor:   13.807


  60 in total

1.  Unfolding of titin domains explains the viscoelastic behavior of skeletal myofibrils.

Authors:  A Minajeva; M Kulke; J M Fernandez; W A Linke
Journal:  Biophys J       Date:  2001-03       Impact factor: 4.033

2.  Dynamics and folding of single two-stranded coiled-coil peptides studied by fluorescent energy transfer confocal microscopy.

Authors:  D S Talaga; W L Lau; H Roder; J Tang; Y Jia; W F DeGrado; R M Hochstrasser
Journal:  Proc Natl Acad Sci U S A       Date:  2000-11-21       Impact factor: 11.205

3.  Segmented nanofibers of spider dragline silk: atomic force microscopy and single-molecule force spectroscopy.

Authors:  E Oroudjev; J Soares; S Arcdiacono; J B Thompson; S A Fossey; H G Hansma
Journal:  Proc Natl Acad Sci U S A       Date:  2002-04-16       Impact factor: 11.205

4.  Unbinding process of adsorbed proteins under external stress studied by atomic force microscopy spectroscopy.

Authors:  C Gergely; J Voegel; P Schaaf; B Senger; M Maaloum; J K Hörber; J Hemmerlé
Journal:  Proc Natl Acad Sci U S A       Date:  2000-09-26       Impact factor: 11.205

5.  Unfolding pathways of native bacteriorhodopsin depend on temperature.

Authors:  Harald Janovjak; Max Kessler; Dieter Oesterhelt; Hermann Gaub; Daniel J Müller
Journal:  EMBO J       Date:  2003-10-01       Impact factor: 11.598

6.  Multi-bead-and-spring model to interpret protein detachment studied by AFM force spectroscopy.

Authors:  Csilla Gergely; Joseph Hemmerlé; Pierre Schaaf; J K Heinrich Hörber; Jean-Claude Voegel; Bernard Senger
Journal:  Biophys J       Date:  2002-08       Impact factor: 4.033

7.  Stability of bacteriorhodopsin alpha-helices and loops analyzed by single-molecule force spectroscopy.

Authors:  Daniel J Müller; Max Kessler; Filipp Oesterhelt; Clemens Möller; Dieter Oesterhelt; Hermann Gaub
Journal:  Biophys J       Date:  2002-12       Impact factor: 4.033

8.  Force spectroscopy of collagen fibers to investigate their mechanical properties and structural organization.

Authors:  Thomas Gutsmann; Georg E Fantner; Johannes H Kindt; Manuela Venturoni; Signe Danielsen; Paul K Hansma
Journal:  Biophys J       Date:  2004-05       Impact factor: 4.033

9.  Simultaneous topography and recognition imaging using force microscopy.

Authors:  Cordula M Stroh; Andreas Ebner; Manfred Geretschläger; Günter Freudenthaler; Ferry Kienberger; A S M Kamruzzahan; Sandra J Smith-Gill; Hermann J Gruber; Peter Hinterdorfer
Journal:  Biophys J       Date:  2004-09       Impact factor: 4.033

10.  Ligand binding modulates the mechanical stability of dihydrofolate reductase.

Authors:  Sri Rama Koti Ainavarapu; Lewyn Li; Carmen L Badilla; Julio M Fernandez
Journal:  Biophys J       Date:  2005-08-12       Impact factor: 4.033

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