AbstractThe recently solved structures of the protein elongation factor complexes, EF-Tu–GDPNP–phenylalanyl-tRNA and EF-T–Ts, complete the atomic profile of four EF-Tu conformational states. As a set, the three-dimensional structures suggest an atomic model for movement during protein elongation and, by molecular mimicry with EF-G, translocation as well
Protein synthesis in the cell is performed on ribosomes, large ribonucleoprotein particles, which in...
AbstractRecent results from cryo-electron microscopy have shown that substantial structural rearrang...
Elongation factor Tu (EF-Tu), bound to GTP, delivers aminoacyl-tRNA (aa-tRNA) as a ternary complex (...
AbstractThe recently solved structures of the protein elongation factor complexes, EF-Tu–GDPNP–pheny...
AbstractThe elongation cycle of protein synthesis on ribosomes is catalyzed by the elongation factor...
The sequential addition of amino acids to a growing polypeptide chain is carried out by the ribosome...
AbstractProtein biosynthesis is controlled by a number of proteins external to the ribosome. Of thes...
AbstractElongation factor (EF) Tu delivers aminoacyl-tRNAs to the actively translating bacterial rib...
Elongation factor Tu (EF-Tu) is a G-protein which, in its active GTP conformation, protects and carr...
AbstractPart of the structure of translational elongation factor G, in a complex with GDP, resembles...
Protein biosynthesis is performed on ribosomes. The ribosome is a complex of ribosomal RNA and prote...
AbstractEvidence is presented for a new role for elongation factor EF-Tu. This involves conformation...
During translation elongation, amino acid residues are repetitively added to the growing nascent pep...
This PhD thesis describes several studies into the structure and function of Escherichia coli Elonga...
In all living organisms, translation of genetic information to proteins takes place on the ribosome....
Protein synthesis in the cell is performed on ribosomes, large ribonucleoprotein particles, which in...
AbstractRecent results from cryo-electron microscopy have shown that substantial structural rearrang...
Elongation factor Tu (EF-Tu), bound to GTP, delivers aminoacyl-tRNA (aa-tRNA) as a ternary complex (...
AbstractThe recently solved structures of the protein elongation factor complexes, EF-Tu–GDPNP–pheny...
AbstractThe elongation cycle of protein synthesis on ribosomes is catalyzed by the elongation factor...
The sequential addition of amino acids to a growing polypeptide chain is carried out by the ribosome...
AbstractProtein biosynthesis is controlled by a number of proteins external to the ribosome. Of thes...
AbstractElongation factor (EF) Tu delivers aminoacyl-tRNAs to the actively translating bacterial rib...
Elongation factor Tu (EF-Tu) is a G-protein which, in its active GTP conformation, protects and carr...
AbstractPart of the structure of translational elongation factor G, in a complex with GDP, resembles...
Protein biosynthesis is performed on ribosomes. The ribosome is a complex of ribosomal RNA and prote...
AbstractEvidence is presented for a new role for elongation factor EF-Tu. This involves conformation...
During translation elongation, amino acid residues are repetitively added to the growing nascent pep...
This PhD thesis describes several studies into the structure and function of Escherichia coli Elonga...
In all living organisms, translation of genetic information to proteins takes place on the ribosome....
Protein synthesis in the cell is performed on ribosomes, large ribonucleoprotein particles, which in...
AbstractRecent results from cryo-electron microscopy have shown that substantial structural rearrang...
Elongation factor Tu (EF-Tu), bound to GTP, delivers aminoacyl-tRNA (aa-tRNA) as a ternary complex (...