倪忠，副研究员，硕导
【学历简介】
2004-2007年浙江理工大学生物化学与分子生物学硕士。
2007-2011年浙江大学化学博士。
【研究领域】
1.脂肪酶催化机理
2.氧化还原酶催化功能及机理
3.生物大分子计算模拟
【科研项目】
1.国家青年自然科学基金（Nos.31200602）
2.国家博士后二等资助（Nos.2012M521001）
3.江苏大学人才基金（Nos.1281330021）
【发表论文】
1.Ni Z,et. al. A Combination of Computational and Experimental Approaches to Investigate the Binding Behavior ofB.subLipase A Mutants with SubstratepNPP.Mol. Inform.2011, 30: 359-367.
2.Ni Z,et. al.Integrating In Silico and In Vitro Approaches to Dissect the Stereoselectivity of Bacillus subtilis Lipase A towards Ketoprofen Vinyl Ester.Chem. Biol. Drug Des.2011, 78: 301-308.
3.Ni Z,et. al.Insight into substituent effects in Cal-B catalyzed transesterification by combining experimental and theoretical approaches.J. Mol. Model. 2013, 19, 349-358.
4.Ni Z,et. al.Just an additional hydrogen bond can dramatically reduce the catalytic activity ofB. sublipase A I12T mutant: an integration of computational modeling and experimental analysis. Comput. Biol. Med. 2013, 43: 1882-1888.
5.Ni Z,et. al.Why is substrate peptide binding unsusceptible to multidrug-resistant mutations in HIV-1 protease? A structural and energetic analysis.Int. J. Pept. Res. Ther.(In press, DOI: 10.1007/s10989-013-9365-9).
6.Ni Z,et. al.Insight into molecular mechanism underlying the transesterification catalyzed by penicillin G amidase (PGA) using a combination protocol of experimental and theoretical analyses.Mol. Simul.(In press, DOI: 10.1080/08927022.2013.850500).
7. Ning JH, Chen WW, Li JJ, Peng ZX, Wang JH,Ni Z*.Structural and energetic insights into sequence-specific interaction in DNA–drug recognition: development of affinity predictor and analysis of binding selectivity.J Mol Model. 2013, 19: 1573-1582.
8. Jin R, Ma Y, Qin L,Ni Z*. Structure-based prediction of domain-peptide binding affinity by dissecting residue interaction profile at complex interface: a case study on CAL PDZ domain,Protein Pept. Lett.2013, 20: 1018-1028.
9. Chen HY, Sun TY, Chen HZ, Tian R, Zhan TX, Chen Z,Ni Z*.Structural and energetic insights into the selective interactions of monoacylglycerol lipase with its natural substrate and small-molecule inhibitors.Med. Chem. Res.(In press, DOI: 10.1007/s00044-013-0832-9).
10.Jin X, Liu B,Ni Z,et. al.A novel control of enzymatic enantioselectivity through the racemic temperature influenced by reaction media.Enzyme Micro. Tech.2011, 48: 454-457.
