Temperature and chemical denaturant dependence of forced unfolding of titin I27.

Temperature and chemical denaturant dependence of forced unfolding of titin I27.
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DOI:
10.1021/jp9002356
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发表时间:
2009-08-06
期刊:
The journal of physical chemistry. B
影响因子:
--
通讯作者:
Kiang CH
Kiang CH
中科院分区:
其他
文献类型:
--
作者:
Botello E;Harris NC;Sargent J;Chen WH;Lin KJ;Kiang CH

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Single-molecule force measurement opens a new door for investigating detailed biomolecular interactions and their thermodynamic properties by pulling molecules apart while monitoring the force exerted on them. Recent advances in the nonequilibrium work theorem allows one to determine the free energy landscapes of these events. Such information is valuable for understanding processes such as protein and RNA folding and receptor-ligand binding. Here we used force as a physical parameter under the traditional chemical and temperature denaturing environment, to alter the protein folding energy landscape and compared the change in unfolding free energy barrier of the I27 domain of human cardiac titin. We found that the trends in protein unfolding free energy barriers are consistent for single-molecule force measurements and bulk chemical and temperature studies. The results suggest that the information from single-molecule pulling experiments are meaningful and useful for understanding the mechanism of folding of titin I27.
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