How to fold intricately: using theory and experiments to unravel the properties of knotted proteins

被引:77
作者
Jackson, Sophie E. [1 ]
Suma, Antonio [2 ]
Micheletti, Cristian [2 ]
机构
[1] Univ Cambridge, Dept Chem, Cambridge CB2 1EW, England
[2] Scuola Int Super Studi Avanzati, SISSA, Via Bonomea 265, I-34136 Trieste, Italy
关键词
TOPOLOGICALLY COMPLEX PROTEINS; INFRARED FLUORESCENT PROTEIN; TRANSFER-RNA; ENERGY LANDSCAPE; TREFOIL KNOT; ACTIVE-SITE; MECHANISM; CONFORMATIONS; STATISTICS; ENZYME;
D O I
10.1016/j.sbi.2016.10.002
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Over the years, advances in experimental and computational methods have helped us to understand the role of thermodynamic, kinetic and active (chaperone-aided) effects in coordinating the folding steps required to achieving a knotted native state. Here, we review such developments by paying particular attention to the complementarity of experimental and computational studies. Key open issues that could be tackled with either or both approaches are finally pointed out.
引用
收藏
页码:6 / 14
页数:9
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