Shuai Wei
University of Michigan
22 Papers
166 Citations
Shuai Wei is an academic researcher from University of Michigan. The author has contributed to research in topics: Graphene & Catalysis. The author has an hindex of 14, co-authored 22 publications. Previous affiliations of Shuai Wei include Brigham Young University.
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Papers
CHARMM-GUI Input Generator for NAMD, Gromacs, Amber, Openmm, and CHARMM/OpenMM Simulations using the CHARMM36 Additive Force Field
Jumin Lee,Xi Cheng,Jason M. Swails,Min Sun Yeom,Peter Eastman,Justin A. Lemkul,Shuai Wei,Joshua Buckner,Jong Cheol Jeong,Yifei Qi,Sunhwan Jo,Vijay S. Pande,David A. Case,Charles L. Brooks,Alexander D. MacKerell,Jeffery B. Klauda,Wonpil Im +16 more
TL;DR: The optimal simulation protocol for each program has been implemented in CHARMM-GUI and is expected to be applicable to the remainder of the additive C36 FF including the proteins, nucleic acids, carbohydrates, and small molecules.
3.3K
Molecular Interactions between Graphene and Biological Molecules
TL;DR: It was found that peptide interactions with graphene depend on the competition between both planar and hydrophilic residues in the peptide, which allows peptides to adopt optimized structure and exhibit excellent activity for nanobio-technological applications.
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Investigating the Effect of Two-Point Surface Attachment on Enzyme Stability and Activity.
Xingquan Zou,Shuai Wei,Somayesadat Badieyan,McKenna Schroeder,Joshua Jasensky,Charles L. Brooks,E. Neil G. Marsh,Zhan Chen +7 more
TL;DR: This research develops a generally applicable and systematic approach using a combination of simulation and experimental methods to rationally select protein immobilization sites for the optimization of surface-immobilized enzyme activity and stability.
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Control of Protein Conformation and Orientation on Graphene.
TL;DR: Immunoglobulin G (IgG) antibody-binding domain of protein G (protein GB1) was studied to demonstrate how it can preserve the protein native structure and control the protein orientation on graphene surface by redesigning protein mutants.
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Effects of Peptide Immobilization Sites on the Structure and Activity of Surface-Tethered Antimicrobial Peptides
Yaoxin Li,Shuai Wei,Jianfeng Wu,Joshua Jasensky,Chuanwu Xi,Honglin Li,Yanmei Xu,Qian Wang,E. Neil G. Marsh,Charles L. Brooks,Zhan Chen +10 more
TL;DR: Results from MSI-78, an antimicrobial peptide, chemically immobilized via the N- or C-terminus (MSI-78n), demonstrate that the attachment site influences the structure and behavior of surface-bound peptides.
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