Haibin Su received his Ph.D. from Stony Brook University (USA) in condensed matter theory and performed his thesis projects at BrookhavenN ational Laboratory,f ollowed by at hree-year stint at Caltech (USA) as ap ostdoctoral scholar in Professor William Goddard's group. He had been af aculty member at Nanyang Technological University (Singapore)s ince 2005, prior to joining The Hong Kong University of Science and Technology in 2018. His research interests include methodology development for characterizing structural, energetic, kinetic, and dynamic properties and functions of complex physical,c hemical, and biological systems at multiple spatial and temporal scales.
Haibin Su received his Ph.D. from Stony Brook University (USA) in condensed matter theory and performed his thesis projects at BrookhavenN ational Laboratory,f ollowed by at hree-year stint at Caltech (USA) as ap ostdoctoral scholar in Professor William Goddard's group. He had been af aculty member at Nanyang Technological University (Singapore)s ince 2005, prior to joining The Hong Kong University of Science and Technology in 2018. His research interests include methodology development for characterizing structural, energetic, kinetic, and dynamic properties and functions of complex physical,c hemical, and biological systems at multiple spatial and temporal scales.
During the ongoing CoVID-19 epidemic, the continuous genomic evolution of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has been generating new variants with enhanced transmissibility and immune escape. Being one key target of antibodies, mutations of the spike glycoprotein play a vital role in the trajectory of virus evasion. Here, we present a time-resolved statistical method, dynamic expedition of leading mutations (deLemus), to analyze the evolution dynamics of the spike protein. Together with analysis on single amino-acid polymorphism (SAP), we proposed one L-index to quantify the mutation strength of each amino acid for unravelling mutation pattern of spike glycoprotein. The sites of interest (SOI) with high L-index hold great promise to detect potential signal of emergent variants.
Ebola virus is a highly lethal¯lovirus, claimed thousands of people in its recent outbreak. Seven viral proteins constitute ebola viral structure, and four of them (nucleoprotein (NP), polymerase L, VP35 and VP30) participate majorly in viral replication and transcription. We have elucidated a conformation change of NP cleft by VP35 NP-binding protein domains through superimposing two experimental NP structure images and discussed the function of this conformation change in the replication and transcription with polymerase complex (L, VP35 and VP30). The important roles of VP30 in viral RNA synthesis have also been discussed. A \tapping" model has been proposed in this paper for a better understanding of the interplay among the four viral proteins (NP, polymerase L, VP35 and VP30). Moreover, we have pinpointed some key residue changes on NP (both NP N-and C-terminal) and L between Reston and Zaire by computational studies. Together, this paper provides a description of interactions among ebola viral proteins (NP, L, VP35, VP30 and VP40) in viral replication and transcription, and sheds light on the complex system of viral reproduction.
scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.