Science China Chemistry

, Volume 57, Issue 12, pp 1615–1624 | Cite as

Tightening up the structure, lighting up the pathway: application of molecular constraints and light to manipulate protein folding, self-assembly and function

  • Beatrice N. Markiewicz
  • Robert M. Culik
  • Feng Gai
Reviews Special Issue Biophysical Chemistry


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.


protein folding aggregation self-assembly cross-linker phototrigger light-activation 


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Copyright information

© Science China Press and Springer-Verlag Berlin Heidelberg 2014

Authors and Affiliations

  • Beatrice N. Markiewicz
    • 1
  • Robert M. Culik
    • 2
  • Feng Gai
    • 1
  1. 1.Department of ChemistryUniversity of PennsylvaniaPennsylvaniaUSA
  2. 2.Department of Biochemistry and BiophysicsUniversity of PennsylvaniaPennsylvaniaUSA

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