Literature DB >> 12324438

Plastic deformation of protein monolayers.

Mukta Singh-Zocchi1, Jeungphill Hanne, Giovanni Zocchi.   

Abstract

Globular proteins are peculiar solids that display both local stability of their conformation and the ability to undergo large cooperative changes of shape (conformational changes). If one forces a large deformation of the molecule, such that the structure is necessarily changed, it is not obvious whether the deformed globule can still remain a solid or whether it will melt. Is it possible to plastically deform a protein? Here we investigate this question with a micro-mechanical experiment on a small region (approximately 10 molecules) of a protein monolayer adsorbed on a rigid surface. For the two proteins studied, albumin and myoglobin, we observed that the molecules can be substantially deformed (approximately 1-2 nm deformation) by comparatively small stresses applied for sufficiently long times. The deformation is irreversible, and the protein remains in the solid state (i.e., displays a nonzero shear modulus). The dynamics of the deformation is approximately logarithmic in time, similar to creep in solids. These results show that globular proteins adsorbed on a surface can be plastically deformed.

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Year:  2002        PMID: 12324438      PMCID: PMC1302309          DOI: 10.1016/S0006-3495(02)73981-7

Source DB:  PubMed          Journal:  Biophys J        ISSN: 0006-3495            Impact factor:   4.033


  25 in total

1.  Osmotic pressure contribution of albumin to colloidal interactions.

Authors:  M Singh-Zocchi; A Andreasen; G Zocchi
Journal:  Proc Natl Acad Sci U S A       Date:  1999-06-08       Impact factor: 11.205

2.  Functionalisation of Si/SiO2 and glass surfaces with ultrathin dextran films and deposition of lipid bilayers.

Authors:  G Elender; M Kühner; E Sackmann
Journal:  Biosens Bioelectron       Date:  1996       Impact factor: 10.618

3.  Energy landscapes of receptor-ligand bonds explored with dynamic force spectroscopy.

Authors:  R Merkel; P Nassoy; A Leung; K Ritchie; E Evans
Journal:  Nature       Date:  1999-01-07       Impact factor: 49.962

4.  Effect of substrate roughness on D spacing supports theoretical resolution of vapor pressure paradox.

Authors:  S Tristram-Nagle; H I Petrache; R M Suter; J F Nagle
Journal:  Biophys J       Date:  1998-03       Impact factor: 4.033

5.  In situ observation of streptavidin-biotin binding on an immunoassay well surface using an atomic force microscope.

Authors:  S Allen; J Davies; A C Dawkes; M C Davies; J C Edwards; M C Parker; C J Roberts; J Sefton; S J Tendler; P M Williams
Journal:  FEBS Lett       Date:  1996-07-22       Impact factor: 4.124

6.  Proteins unfold in steps.

Authors:  G Zocchi
Journal:  Proc Natl Acad Sci U S A       Date:  1997-09-30       Impact factor: 11.205

7.  Behavior of supercoiled DNA.

Authors:  T R Strick; J F Allemand; D Bensimon; V Croquette
Journal:  Biophys J       Date:  1998-04       Impact factor: 4.033

8.  Reversible unfolding of individual titin immunoglobulin domains by AFM.

Authors:  M Rief; M Gautel; F Oesterhelt; J M Fernandez; H E Gaub
Journal:  Science       Date:  1997-05-16       Impact factor: 47.728

9.  Folding-unfolding transitions in single titin molecules characterized with laser tweezers.

Authors:  M S Kellermayer; S B Smith; H L Granzier; C Bustamante
Journal:  Science       Date:  1997-05-16       Impact factor: 47.728

10.  Elasticity and unfolding of single molecules of the giant muscle protein titin.

Authors:  L Tskhovrebova; J Trinick; J A Sleep; R M Simmons
Journal:  Nature       Date:  1997-05-15       Impact factor: 49.962

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  1 in total

1.  Single-molecule detection of DNA hybridization.

Authors:  Mukta Singh-Zocchi; Sanhita Dixit; Vassili Ivanov; Giovanni Zocchi
Journal:  Proc Natl Acad Sci U S A       Date:  2003-06-13       Impact factor: 11.205

  1 in total

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