Nothing Special   »   [go: up one dir, main page]

Duisterwinkel et al., 1984 - Google Patents

Specific alterations of the EF‐Tu polypeptide chain considered in the light of its three‐dimensional structure.

Duisterwinkel et al., 1984

View PDF
Document ID
6373324827319737368
Author
Duisterwinkel F
Kraal B
De Graaf J
Talens A
Bosch L
Swart G
Parmeggiani A
La Cour T
Nyborg J
Clark B
Publication year
Publication venue
The EMBO Journal

External Links

Snippet

Specific alterations of the elongation factor Tu (EF‐Tu) polypeptide chain have been identified in a number of mutant species of this elongation factor. In two species, Ala‐375, located on domain II, was found by amino acid analysis to be replaced by Thr and Val …
Continue reading at www.embopress.org (PDF) (other versions)

Classifications

    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
    • C07K14/46—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
    • C07K14/47—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals
    • C07K14/4701—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals not used
    • C07K14/4702—Regulators; Modulating activity
    • C07K14/4703—Inhibitors; Suppressors
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • C07K14/195—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria
    • C07K14/24—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria from Enterobacteriaceae (F), e.g. Citrobacter, Serratia, Proteus, Providencia, Morganella, Yersinia
    • C07K14/245—Escherichia (G)
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
    • C07K14/575—Hormones
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
    • C07K14/43504—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from invertebrates
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K1/00—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length
    • C07K1/107—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length by chemical modification of precursor peptides
    • C07K1/1072—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length by chemical modification of precursor peptides by covalent attachment of residues or functional groups
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12N—MICRO-ORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING OR MAINTAINING MICRO-ORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/14—Hydrolases (3)
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K2319/00—Fusion polypeptide
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12N—MICRO-ORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING OR MAINTAINING MICRO-ORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
    • C12N15/09—Recombinant DNA-technology

Similar Documents

Publication Publication Date Title
Duisterwinkel et al. Specific alterations of the EF‐Tu polypeptide chain considered in the light of its three‐dimensional structure.
Lupas et al. Structural features of 26S and 20S proteasomes
US4839293A (en) DNA encoding streptavidin, streptavidin produced therefrom, fused polypeptides which include amino acid sequences present in streptavidin and uses thereof
Clark-Lewis et al. Chemical synthesis, purification, and characterization of two inflammatory proteins, neutrophil activating peptide 1 (interleukin-8) and neutrophil activating peptide 2
Villarejo et al. β-Galactosidase from termination and deletion mutant strains
Bestor et al. Cloning and sequencing of a cDNA encoding DNA methyltransferase of mouse cells: the carboxyl-terminal domain of the mammalian enzymes is related to bacterial restriction methyltransferases
Beyreuther et al. The Phosphoenolpyruvate‐Dependent Phosphotransferase System of Staphylococcus aureus: 1. Amino‐Acid Sequence of the Phosphocarrier Protein HPr
Lillehoj et al. Purification and structural characterization of the putative gag-pol protease of human immunodeficiency virus
Cameron et al. Purification to homogeneity and amino acid sequence analysis of two anionic species of human interleukin 1.
Copeland et al. Complete amino acid sequence of human T-cell leukemia virus structural protein p15
Stone et al. The amino acid sequence of the trimethoprim-resistant dihydrofolate reductase specified in Escherichia coli by R-plasmid R67.
Nagasawa et al. Determination of the cleavage site involved in C-terminal processing of penicillin-binding protein 3 of Escherichia coli
Yanofsky et al. Tryptophan synthetase α chain positions affected by mutations near the ends of the genetic map of trpA of Escherichia coli
Aiba et al. Isolation and characterization of the amino and carboxyl proximal fragments of the adenosine cyclic 3', 5'-phosphate receptor protein of Escherichia coli
Biemann Sequencing of proteins
Yen et al. Bacteriophage f1 gene II and X proteins. Isolation and characterization of the products of two overlapping genes.
Funatsu et al. Ribosomal proteins. XXXVII. Determination of allelle types and amino acid exchanges in protein S12 of three streptomycin-resistant mutants of Escherichia coli
Tsunasawa et al. Methionine aminopeptidase from the hyperthermophilic Archaeon Pyrococcus furiosus: molecular cloning and overexperssion in Escherichia coli of the gene, and characteristics of the enzyme
Subramanian et al. Fragments of Ribosomal Protein S1 and Its Mutant Form m1‐S1: Localization of Nucleic‐Acid‐Binding Domain in the Middle Region of S1
Piepersberg et al. Genetic position and amino acid replacements of several mutations in ribosomal protein S5 from Escherichia coli
Reiche et al. Staphylococcal phosphoenolpyruvate-dependent phosphotransferase system: purification and characterization of the mannitol-specific enzyme IIImtl of Staphylococcus aureus and Staphylococcus carnosus and homology with the enzyme IImtl of Escherichia coli
Strydom et al. An Angiogenic Protein from Bovine Serum and Milk—Purification and Primary Structure of Angiogenin‐2
Metz-Boutigue et al. Crosslinking of elongation factor Tu to tRNAPhe by trans‐diamminedichloroplatinum (II) Characterization of two crosslinking sites on EF‐Tu
Baron et al. Antibodies against a synthetic peptide of the poliovirus replicase protein: reaction with native, virus-encoded proteins and inhibition of virus-specific polymerase activities in vitro
Kahan et al. The structural gene for the ribosomal protein S18 in Escherichia coli: II. Chemical studies on the protein S18 having an altered electrophoretic mobility