The Effect of Protein Complexation on the Mechanical Stability of Im9

Force mode microscopy can be used to examine the effect of mechanical manipulation on the noncovalent interactions that stabilize proteins and their complexes. Here we describe the effect of complexation by the high affinity protein ligand E9 on the mechanical resistance of the simple four-helical p...

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Bibliographic Details
Published in:Biophysical journal 2007-05, Vol.92 (9), p.L79-L81
Main Authors: Hann, Eleanore, Kirkpatrick, Nadine, Kleanthous, Colin, Smith, D. Alastair, Radford, Sheena E., Brockwell, David J.
Format: Article
Language:English
Subjects:
Amino acids
Biochemistry
Biomechanical Phenomena
Biophysical Letters
Colicins - chemistry
Colicins - ultrastructure
Elasticity
Escherichia coli Proteins - chemistry
Escherichia coli Proteins - ultrastructure
Microscopy, Atomic Force - methods
Multiprotein Complexes - chemistry
Multiprotein Complexes - ultrastructure
Peptides
Protein Conformation
Protein Denaturation
Proteins
Reaction kinetics
Stress, Mechanical
Thermodynamics
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Summary:Force mode microscopy can be used to examine the effect of mechanical manipulation on the noncovalent interactions that stabilize proteins and their complexes. Here we describe the effect of complexation by the high affinity protein ligand E9 on the mechanical resistance of the simple four-helical protein, Im9. When concatenated into a construct of alternating I27 domains, Im9 unfolded below the thermal noise limit of the instrument (∼20 pN). Complexation of E9 had little effect on the mechanical resistance of Im9 (unfolding force ∼30 pN) despite the high avidity of this complex ( K d ∼10 fM).
ISSN:0006-3495
1542-0086
DOI:10.1529/biophysj.106.102475