Authors:

Ryan Rushing

Date Created:

Not specified

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About Paper:

Proteins are large molecules that perform both structural and functional roles in live cells. Key to their abilities, most of these long polymeric molecules spontaneously fold into specific 3-dimensional structures. Because of this, much work has been done to study the mechanics and thermodynamics of the 3-dimensional, folded structure of proteins. Using laboratory-built magnetic tweezers, we found previously that the difference in free energy between the folded and unfolded forms of Protein L held under tension is 6.5 kBT, in media with 150 mM NaCl, pH 7.4, and R.T. To further probe the folding-unfolding transition of Protein L, here we extend the previous study to observe the effect of varying environmental conditions on these transitions under tension. Specifically, we have preliminary data that suggests that an increase in environmental monovalent salt concentration does not significantly affect the free energy difference between the folded and unfolded form of protein L but does allow for more frequent hops between the two states implying a lowering of the energy of an intermediate, transition state along the unfolding pathway. This current study continues and extends this work to probe modifications to the free energy landscape along the tension-induced unfolding pathway due to an increase in environmental salts.

Source:

Purdue University / 2023

Topics:

No topics listed

Co-authors:

Ryan Rushing