Protein melting point - thermal denaturation
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Protein melting point - Case study

Many proteins show profound changes when exposed to solution conditions, with the most extreme structure change being thermal denaturation. When a protein is heated above its characteristic thermal stability point (protein melting point), significant unfolding leads to exposed hydrophobic chains and can cause severe, nonreversible aggregation.

Light scattering is ideal for studying the protein melting point phenomenon as the technique is exquisitely sensitive to large scattering objects such as aggregates and denatured protein. Similar structure changes may happen over time, pH, ionic strength and changes in various other solution conditions, and light scattering again is an ideal tool to quickly assess the condition of the molecule in solution.

 
  
Presentations:
 
 
On demand presentation on Protein Melting Point.
Proteins are charged biomolecules that can fold into compact structures that are very sensitive to solution conditions. As an extreme case, thermal denaturation can lead to irreversible loss of structure and function of the molecule. Thermal denaturation typically leads to an increase in size that can be monitored by dynamic light scattering. At the protein melting point, a marked increase in hydrodynamic size and scattering intensity is observed. This protein melting point temperature is indicative of the thermal stability of a protein. Modifications (such as glycosylation) can influence the stability and are easily observed using dynamic light scattering.
 
   
Application note on Characterization of Protein Melting Point.
Proteins are composed of polypeptide chains with unique 3-dimensional structures in the native state. These structures are stabilized by a combination of electrostatic and hydrophobic interactions, combined with a large degree of flexibility inside the structure of the molecule. If solution conditions change, denaturation or unfolding can quickly occur, along with a subsequent change in size. The sensitivity of dynamic light scattering is ideally suited for monitoring the stability of a protein to denaturing conditions. The protein melting point temperature is indicative of the thermal stability of a protein. Modifications (such as glycosylation) can influence the stability and are easily observed with dynamic light scattering.