Structural and conformational behavior of MurE ligase from Salmonella enterica serovar Typhi at different temperature and pH conditions

Keyphrases

• Salmonella Typhi (S. Typhi) 100%
• Ligase 100%
• Structural Behavior 100%
• Conformational Behavior 100%
• MurE Ligase 100%
• Environmental Conditions 50%
• Fluorescence Spectroscopy 25%
• Structural Change 25%
• Amino Acid Residues 25%
• Bacterial Pathogenesis 25%
• Conformational Change 25%
• Enzyme Activity 25%
• Temperature Effect 25%
• Homology Modeling 25%
• Spectroscopic Techniques 25%
• Alkaline pH 25%
• Acidic pH 25%
• Protein Stability 25%
• PH Dependence 25%
• Secondary Structural Elements 25%
• Unfolded State 25%
• Substrate Binding 25%
• Far-UV CD 25%
• Near-UV 25%
• Differential Scanning Calorimetry 25%
• Dynamic State 25%
• Molten Globule State 25%
• Differential Scanning Fluorimetry 25%
• Peptidoglycan Synthesis 25%
• Ionization State 25%
• ANS Fluorescence 25%
• Catalytic Amino Acids 25%
• Meso-diaminopimelic Acid 25%
• Conformational Modification 25%

Biochemistry, Genetics and Molecular Biology

• Ligase 100%
• Salmonella Enterica Serovar Typhi 100%
• Dynamics 14%
• Anabolism 14%
• Enzyme 14%
• Amino Acids 14%
• Precursor 14%
• Conformational Change 14%
• Enzyme Activity 14%
• Conformation 14%
• Spectroscopy 14%
• Alkalinity 14%
• Protein Stability 14%
• Molten Globule 14%
• Differential Scanning Calorimetry 14%
• Peptidoglycan 14%
• Fluorescence Spectroscopy 14%