期刊论文

Hirota, Shun;Lin, Ying-Wu

英文

JOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY

0949-8257

2018

23

1

7-25

10.1007/s00775-017-1506-8

JSPSMinistry of Education, Culture, Sports, Science and Technology, Japan (MEXT)Japan Society for the Promotion of Science [JP26288080, JP16H00839]; National Natural Science Foundation of ChinaNational Natural Science Foundation of China (NSFC) [31370812]; Hunan Provincial Natural Science FoundationNatural Science Foundation of Hunan Province [2015JJ1012]; Grants-in-Aid for Scientific ResearchMinistry of Education, Culture, Sports, Science and Technology, Japan (MEXT)Japan Society for the Promotion of ScienceGrants-in-Aid for Scientific Research (KAKENHI) [16H00839] Funding Source: KAKEN

本校为通讯机构

Noncovalent weak interactions [hydrophobic interaction and hydrogen (H)-bond] play crucial roles in controlling the functions of biomolecules, and thus have been used to design artificial metalloproteins/metalloenzymes during the past few decades. In this review, we focus on the recent progresses in protein design by tuning the noncovalent interactions, including hydrophobic and H-bonding interactions. The topics include redesign and reuse of the heme pocket and other protein scaffolds, design of the heme protein interface, and de novo design of metalloproteins. The informations not only give ...