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Methods in Enzymology, ISSN 0076-6879, 2015, Volume 565, pp. 311 - 345
This chapter describes the cell-free protein synthesis method, using an Escherichia coli cell extract. This is a cost-effective method for milligram-scale... 
Protein complex | Membrane protein | NMR | Amino acid | Site specific | Cell-free protein synthesis | Mammalian protein | Stable isotope labeling | Amino acid selective | Escherichia coli cell extract | Isotope Labeling | Ligands | Molecular Weight | Cell-Free System | Escherichia coli Proteins - biosynthesis | Escherichia coli - metabolism
Journal Article
Journal Article
Journal Article
Methods in enzymology, 2015, Volume 565, pp. 311 - 345
This chapter describes the cell-free protein synthesis method, using an Escherichia coli cell extract. This is a cost-effective method for milligram-scale... 
Protein complex | Membrane protein | NMR | Amino acid | Site specific | Cell-free protein synthesis | Mammalian protein | Stable isotope labeling | Amino acid selective | Escherichia coli cell extract
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 11/2016, Volume 113, Issue 46, pp. 12997 - 13002
The 3C-like protease (3CL ) of severe acute respiratory syndrome coronavirus (SARS-CoV) cleaves 11 sites in the polyproteins, including its own N- and... 
3CL protease | SARS | Specificity | Subsite cooperativity | Crystal structure | DIMER INTERFACE | TOPOLOGY | SYSTEM | SUITE | COMPLEX | MECHANISM | MULTIDISCIPLINARY SCIENCES | MAIN PROTEASE | DIMERIZATION | SUBSTRATE-SPECIFICITY | subsite cooperativity | CORONAVIRUS 3C-LIKE PROTEASE | specificity | crystal structure | Biological Sciences
Journal Article
Cell Reports, ISSN 2211-1247, 05/2017, Volume 19, Issue 5, pp. 969 - 980
Journal Article
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 2/2012, Volume 109, Issue 9, pp. 3305 - 3310
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 12/2011, Volume 108, Issue 50, pp. 19955 - 19960
V-ATPases function as ATP-dependent ion pumps in various membrane systems of living organisms. ATP hydrolysis causes rotation of the central rotor complex,... 
Proteins | Enterococcus | Thermus | Archaea | Adenosine triphosphatases | Biochemistry | Physiology | Cell membranes | Rotation | Crystal structure | NA+-ATPASE | ENTEROCOCCUS-HIRAE | SUBUNIT-F | MULTIDISCIPLINARY SCIENCES | CRYSTALLOGRAPHY | PERIPHERAL STALK | ROTOR RING | PROTEINS | THERMUS-THERMOPHILUS | CENTRAL STALK | BINDING | Research | Properties | Structure | Prokaryotes | Adenosine triphosphatase | Crystals | Biological Sciences
Journal Article
Journal Article