The current scenario of COVID-19 makes us to think about the devastating diseases that kill so many people every year.Analysis of viral proteins contributes many things that are utterly useful in the evolution of ther...The current scenario of COVID-19 makes us to think about the devastating diseases that kill so many people every year.Analysis of viral proteins contributes many things that are utterly useful in the evolution of therapeutic drugs and vaccines.In this study,sequence and structure of fusion glycoproteins and major surface glycoproteins of respiratory syncytial virus(RSV)were analysed to reveal the stability and transmission rate.RSV A has the highest abundance of aromatic residues.The Kyte–Doolittle scale indicates the hydrophilic nature of RSV A protein which leads to the higher transmission rate of this virus.Intra-protein interactions such as carbonyl interactions,cation-pi,and salt bridges were shown to be greater in RSV A compared to RSV B,which might lead to improved stability.This study discovered the presence of a network aromatic–sulphur interaction in viral proteins.Analysis of ligand binding pocket of RSV proteins indicated that drugs are performing better on RSV B than RSV A.It was also shown that increasing the number of tunnels in RSV A proteins boosts catalytic activity.This study will be helpful in drug discovery and vaccine development.展开更多
Non-specific electrostatics is crucial for structure and stability;recently,it has been argued that psychrophilic proteins may also utilize specific electrostatic interactions.Do psychrophilic proteins increase the nu...Non-specific electrostatics is crucial for structure and stability;recently,it has been argued that psychrophilic proteins may also utilize specific electrostatic interactions.Do psychrophilic proteins increase the number of salt bridges for cold adaptation?Are there any changes that occur in their sequence,which helps them to adapt in an extreme environment?Do intra-protein interactions affect their stability?Is there any special type of intra-protein interaction present in psychrophilic protein structure?This study will give all those answers.Sequences(n~100)and structures of psychrophilic isocitrate dehydrogenase and mesophilic isocitrate dehydrogenase extracted from databases.Sequences had been analyzed in BLOCK and non-BLOCK format.The sequences of psychrophiles and mesophiles create two separate clades.The number of charged and uncharged polar residues is very much high in psychrophilic proteins.The formation of long network aromatic-aromatic interactions and network aromatic-sulfur interactions are very crucial for psychrophilic protein stability.Identification of these types of interactions is also a novelty of this study.Favorable mutation of charged residues with high-energy contributions affects the protein stability.This study will help in protein engineering.展开更多
The current nightmare for the whole world is COVID-19.The occurrence of concentrated pneumonia cases in Wuhan city,Hubei province of China,was first reported on December 30,2019.SARS-CoV first disclosed in 2002 but ha...The current nightmare for the whole world is COVID-19.The occurrence of concentrated pneumonia cases in Wuhan city,Hubei province of China,was first reported on December 30,2019.SARS-CoV first disclosed in 2002 but had not outspread worldwide.After 18 years,in 2020,it reemerged and outspread worldwide as SARS-CoV-2(COVID-19),as the most dangerous virus-creating disease in the world.Is it possible to create a favorable evolution within the short time(18 years)?If possible,then what are those properties or factors that are changed in SARS-CoV-2 to make it undefeated?What are the fundamental differences between SARS-CoV-2 and SARS?The study is one of the initiatives to find out all those queries.Here,four types of protein sequences from SARS-CoV-2 and SARS were retrieved from the database to study their physicochemical and structural properties.Results showed that charged residues are playing a pivotal role in SARS-CoV-2 evolution and contribute to the helix stabilization.The formation of the cyclic salt bridge and other intra-protein interactions specially network aromatic-aromatic interaction also play the crucial role in SAS-CoV-2.This comparative study will help to understand the evolution from SARS to SARS-CoV-2 and helpful in protein engineering.展开更多
文摘The current scenario of COVID-19 makes us to think about the devastating diseases that kill so many people every year.Analysis of viral proteins contributes many things that are utterly useful in the evolution of therapeutic drugs and vaccines.In this study,sequence and structure of fusion glycoproteins and major surface glycoproteins of respiratory syncytial virus(RSV)were analysed to reveal the stability and transmission rate.RSV A has the highest abundance of aromatic residues.The Kyte–Doolittle scale indicates the hydrophilic nature of RSV A protein which leads to the higher transmission rate of this virus.Intra-protein interactions such as carbonyl interactions,cation-pi,and salt bridges were shown to be greater in RSV A compared to RSV B,which might lead to improved stability.This study discovered the presence of a network aromatic–sulphur interaction in viral proteins.Analysis of ligand binding pocket of RSV proteins indicated that drugs are performing better on RSV B than RSV A.It was also shown that increasing the number of tunnels in RSV A proteins boosts catalytic activity.This study will be helpful in drug discovery and vaccine development.
文摘Non-specific electrostatics is crucial for structure and stability;recently,it has been argued that psychrophilic proteins may also utilize specific electrostatic interactions.Do psychrophilic proteins increase the number of salt bridges for cold adaptation?Are there any changes that occur in their sequence,which helps them to adapt in an extreme environment?Do intra-protein interactions affect their stability?Is there any special type of intra-protein interaction present in psychrophilic protein structure?This study will give all those answers.Sequences(n~100)and structures of psychrophilic isocitrate dehydrogenase and mesophilic isocitrate dehydrogenase extracted from databases.Sequences had been analyzed in BLOCK and non-BLOCK format.The sequences of psychrophiles and mesophiles create two separate clades.The number of charged and uncharged polar residues is very much high in psychrophilic proteins.The formation of long network aromatic-aromatic interactions and network aromatic-sulfur interactions are very crucial for psychrophilic protein stability.Identification of these types of interactions is also a novelty of this study.Favorable mutation of charged residues with high-energy contributions affects the protein stability.This study will help in protein engineering.
文摘The current nightmare for the whole world is COVID-19.The occurrence of concentrated pneumonia cases in Wuhan city,Hubei province of China,was first reported on December 30,2019.SARS-CoV first disclosed in 2002 but had not outspread worldwide.After 18 years,in 2020,it reemerged and outspread worldwide as SARS-CoV-2(COVID-19),as the most dangerous virus-creating disease in the world.Is it possible to create a favorable evolution within the short time(18 years)?If possible,then what are those properties or factors that are changed in SARS-CoV-2 to make it undefeated?What are the fundamental differences between SARS-CoV-2 and SARS?The study is one of the initiatives to find out all those queries.Here,four types of protein sequences from SARS-CoV-2 and SARS were retrieved from the database to study their physicochemical and structural properties.Results showed that charged residues are playing a pivotal role in SARS-CoV-2 evolution and contribute to the helix stabilization.The formation of the cyclic salt bridge and other intra-protein interactions specially network aromatic-aromatic interaction also play the crucial role in SAS-CoV-2.This comparative study will help to understand the evolution from SARS to SARS-CoV-2 and helpful in protein engineering.
