Tightening up the structure,lighting up the pathway:Application of molecular constraints and light t

• 作 者: MARKIEWICZBeatriceN[1]CULIKRobertM[2]GAIFeng[1]
• 机 构: Department of Chemistry,University of Pennsylvania,PA,19104,USA
• 出 处: 中国化学会第三届全国生物物理化学会议暨国际华人生物物理化学发展论坛
• 发表日期: 2014年期

　　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 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.