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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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作者 mARKIEWICZ Beatrice N. culik robert m. GAI Feng 《Science China Chemistry》 SCIE EI CAS 2014年第12期1615-1624,共10页
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.Rec... 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. 展开更多
关键词 protein folding aggregation SELF-ASSEMBLY CROSS-LINKER phototrigger light-activation
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