Tightening up the structure, lighting up the pathway: Application of molecular constraints and light to manipulate protein folding, self-assembly and function.
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.
Department of Chemistry, University of Pennsylvania, PA, 19104, USA.
Beatrice N
BN
Markiewicz
Department of Biochemistry and Biophysics, University of Pennsylvania, PA, 19104, USA.
Robert M
RM
Culik
Department of Chemistry, University of Pennsylvania, PA, 19104, USA.
Feng
F
Gai
Protein folding; aggregation; cross-linker; light-activation; phototrigger; self-assembly