The role of Atomic Force microscopy

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DYNAMIC OF BIOMOLECULES AND CELLS 2014

Unfolding the elastomeric protein titin using atomic force microscopy

Why atomic force microscopy is most suited to this task

An essay on the role atomic force microscopy plays in the unfolding of titin and why atomic force microscopy is suited to such experiments

Proteins are a group of molecules, present in the human body (and other living organisms), that have varied functions. They are made up of chains of smaller molecules called amino acids. The amino acids are arranged in long strings, these strings are then folded into shapes to create a functional component.

Proteins have lots of different functions, such as bio-regulation (in the case of hormones). There exist transport proteins that for example move minerals through the body, structural proteins make up the skin, bones and some proteins are catalytic (enzymes).

This essay focusses on an elastomeric protein. An elastomer is an elastic polymer; elastomeric proteins are multi-unit proteins that display elasticity.

Elasticity is ability of a solid material to return to the original form after deformation. The physical origin for elasticity varies per material. In the case of rubber and other elastic polymers, the elasticity arises from the stretching of the polymer chain (when force is applied to it) that the elastic polymer is made of.

To study the elasticity of proteins, a tool has to be used that can measure the force required to make a certain extension of the polymer. One such tool is the atomic force microscope (AFM).

An AFM uses a sharp tip on a cantilever that will deflect when it is brought in close proximity to a surface. The deflection of the cantilever can be measured and the topography of the sample...

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...i, Z. & Kellermayer, M. Individual globular domains and domain unfolding visualized in overstretched titin molecules with atomic force microscopy. PLoS One 9, e85847 (2014).

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