[go: up one dir, main page]
More Web Proxy on the site http://driver.im/

Ubago-Rodríguez et al., 2019 - Google Patents

Structure–function of MamC loop and its effect on the in vitro precipitation of biomimetic magnetite nanoparticles

Ubago-Rodríguez et al., 2019

View PDF
Document ID
16395925652662505294
Author
Ubago-Rodríguez A
Casares Atienza S
Fernández-Vivas A
Peigneux A
Jabalera Y
de la Cuesta-Rivero M
Jimenez-Lopez C
Azuaga Fortes A
Publication year
Publication venue
Crystal Growth & Design

External Links

Snippet

MamC, an integral protein of the magnetosome membrane, has recently been proposed as a strong candidate to produce biomimetic (magnetosome-like) magnetite nanoparticles that could be used as an alternative to magnetosomes in different applications such as …
Continue reading at www.academia.edu (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
    • 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
    • C07K1/113—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 without change of the primary structure
    • C07K1/1136—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 without change of the primary structure by reversible modification of the secondary, tertiary or quarternary structure, e.g. using denaturating or stabilising agents
    • 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
    • C12N15/10—Processes for the isolation, preparation or purification of DNA or RNA
    • C12N15/1034—Isolating an individual clone by screening libraries
    • C12N15/1044—Preparation or screening of libraries displayed on scaffold proteins
    • 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
    • C07K14/705—Receptors; Cell surface antigens; Cell surface determinants
    • 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
    • C07K14/79—Transferrins, e.g. lactoferrins, ovotransferrins
    • 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
    • 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
    • C07K2319/00—Fusion polypeptide
    • C07K2319/01—Fusion polypeptide containing a localisation/targetting motif
    • C07K2319/035—Fusion polypeptide containing a localisation/targetting motif containing a signal for targeting to the external surface of a cell, e.g. to the outer membrane of Gram negative bacteria, GPI- anchored eukaryote proteins

Similar Documents

Publication Publication Date Title
Rawlings Membrane proteins: always an insoluble problem?
Ubago-Rodríguez et al. Structure–function of MamC loop and its effect on the in vitro precipitation of biomimetic magnetite nanoparticles
Aubin-Tam et al. Site-directed nanoparticle labeling of cytochrome c
Song et al. The crystal structure of human eukaryotic release factor eRF1—mechanism of stop codon recognition and peptidyl-tRNA hydrolysis
Schubot et al. Three-dimensional structure of a macromolecular assembly that regulates type III secretion in Yersinia pestis
Hong Toward understanding driving forces in membrane protein folding
Paxman et al. The structure of the bacterial oxidoreductase enzyme DsbA in complex with a peptide reveals a basis for substrate specificity in the catalytic cycle of DsbA enzymes
Lopez-Moreno et al. Magnetite nanoparticles biomineralization in the presence of the magnetosome membrane protein MamC: effect of protein aggregation and protein structure on magnetite formation
Misura et al. Crystal structure and biophysical properties of a complex between the N-terminal SNARE region of SNAP25 and syntaxin 1a
Aravind et al. The βγ-crystallin superfamily contains a universal motif for binding calcium
Rosano et al. Crystal structure and anion binding in the prokaryotic hydrogenase maturation factor HypF acylphosphatase-like domain
Smith et al. Mutation of interfaces in domain‐swapped human βB2‐crystallin
Faraone-Mennella et al. Stability and folding kinetics of structurally characterized cytochrome c-b 562
Bratanov et al. An approach to heterologous expression of membrane proteins. The case of bacteriorhodopsin
Smith et al. Metal selectivity of a Cd-, Co-, and Zn-transporting P1B-type ATPase
Stalmans et al. Addressing the molecular mechanism of longitudinal lamin assembly using chimeric fusions
Nautiyal et al. Design and assessment of an active anti-epidermal growth factor receptor (EGFR) single chain variable fragment (ScFv) with improved solubility
Haupt et al. Local and coupled thermodynamic stability of the two-domain and bifunctional enzyme SlyD from Escherichia coli
Watson et al. Spontaneous self-assembly of engineered armadillo repeat protein fragments into a folded structure
MacGillivray et al. Mutation of the iron ligand His 249 to Glu in the N-lobe of human transferrin abolishes the dilysine “trigger” but does not significantly affect iron release
Weikum et al. The extracellular juncture domains in the intimin passenger adopt a constitutively extended conformation inducing restraints to its sphere of action
Hurtado-Guerrero et al. Molecular mechanism of elongation factor 1A inhibition by a Legionella pneumophila glycosyltransferase
Ouyang et al. Crystal structures of E. coli CcmG and its mutants reveal key roles of the N‐terminal β‐sheet and the fingerprint region
Ukwaththage et al. Purification of tag-free Chlamydia trachomatis Scc4 for structural studies using sarkosyl-assisted on-column complex dissociation
Hennon et al. Cross-linking-based flexibility and proximity relationships between the TM segments of the Escherichia coli YidC