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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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| Published in: | Biophysical journal 2007-05, Vol.92 (9), p.L79-L81 |
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| Main Authors: | , , , , , |
| Format: | Article |
| Language: | English |
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| cites | cdi_FETCH-LOGICAL-c484t-9d097dcc00924124c4e08189dd4354e4577ae0a5af928e4772e3c5047a3872bd3 |
| container_end_page | L81 |
| container_issue | 9 |
| container_start_page | L79 |
| container_title | Biophysical journal |
| container_volume | 92 |
| creator | Hann, Eleanore Kirkpatrick, Nadine Kleanthous, Colin Smith, D. Alastair Radford, Sheena E. Brockwell, David J. |
| description | 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). |
| doi_str_mv | 10.1529/biophysj.106.102475 |
| format | article |
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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
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K
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Alastair</au><au>Radford, Sheena E.</au><au>Brockwell, David J.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The Effect of Protein Complexation on the Mechanical Stability of Im9</atitle><jtitle>Biophysical journal</jtitle><addtitle>Biophys J</addtitle><date>2007-05-01</date><risdate>2007</risdate><volume>92</volume><issue>9</issue><spage>L79</spage><epage>L81</epage><pages>L79-L81</pages><issn>0006-3495</issn><eissn>1542-0086</eissn><abstract>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).</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>17351013</pmid><doi>10.1529/biophysj.106.102475</doi><oa>free_for_read</oa></addata></record> |
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| ispartof | Biophysical journal, 2007-05, Vol.92 (9), p.L79-L81 |
| issn | 0006-3495 1542-0086 |
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| 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 |
| title | The Effect of Protein Complexation on the Mechanical Stability of Im9 |
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