Tightening up the structure,lighting up the pathway: application of molecular constraints and light to manipulate protein folding,self-assembly and function |
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Authors: | Beatrice N. Markiewicz Robert M. Culik Feng Gai |
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Abstract: | Chemical cross-linking provides an effective avenue to reduce the conformational entropy of polypeptide chains and hence has become a popular method to induce or force structural formation in peptides and proteins.Recently,other types of molecular constraints,especially photoresponsive linkers and functional groups,have also found increased use in a wide variety of applications.Herein,we provide a concise review of using various forms of molecular strategies to constrain proteins,thereby stabilizing their native states,gaining insight into their folding mechanisms,and/or providing a handle to trigger a conformational process of interest with light.The applications discussed here cover a wide range of topics,ranging from delineating the details of the protein folding energy landscape to controlling protein assembly and function. |
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Keywords: | protein folding aggregation self-assembly cross-linker phototrigger light-activation |
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