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Complexes protein

Noble M E M, R K Wierenga, A-M Lambeir, F R Opperdoes, W H Thunnissen, K H Kalk, H Groendijk and W G J Hoi 1991. The Adaptability of the Active Site of Trypanosomal Triosephosphate Isomerase as Observed in the Crystal Structures of Three Different Complexes. Proteins Structure, Function and Genetics 10 50-69. [Pg.576]

Nutritional Requirements. The nutrient requirements of mammalian cells are many, varied, and complex. In addition to typical metaboHc requirements such as sugars, amino acids (qv), vitamins (qv), and minerals, cells also need growth factors and other proteins. Some of the proteins are not consumed, but play a catalytic role in the cell growth process. Historically, fetal calf semm of 1—20 vol % of the medium has been used as a rich source of all these complex protein requirements. However, the composition of semm varies from lot to lot, introducing significant variabiUty in manufacture of products from the mammalian cells. [Pg.229]

Mechanism of Dyeing. Wool (qv) is a complex protein polymer based on amino acid building blocks, and the polymer chains are cross-linked by disulfide groups. Amino acids (qv) contain both amino and carboxyUc acid groups and therefore the wool polymer contains both —NH2... [Pg.359]

FIGURE 4.49 Isolation of a complex protein conjugate on Toyopearl HW-50S. Column 22 mm X 83 cm. Sample Fraction from crude Tetrahymena H2A containing the ubiquitin-histone conjugate uH2A. Elution 10 nM HCI. Flow rate 0.1 ml/min. Detection UV at 230 nm. [Pg.156]

H. Yamamoto, T. Manabe and T. Okuyama, Apparatus for coupled high-performance liquid chromatography and capillary electrophoresis in the analysis of complex protein mixtures , 7. Chromatogr. 515 659-666 (1990). [Pg.214]

Structural Formula Complex protein, molecular weight 33,000 Chemical Abstracts Registry No. 9001-00-7... [Pg.183]

Chemical Name Complex protein, molecular weight about 75,000... [Pg.641]

Structural Formula Complex protein structure not precisely defined Chemical Abstracts Registry No. 9008-11 -1... [Pg.822]

Structural Formula Orgotein is a complex protein with a molecular weight of about 33,000. It Is a divalent metal (Mg, Cu, Zn) chelated structure. [Pg.1114]

Electrochemical studies performed in the 7 x Cys-Aspl4 D. afri-canus Fdlll indicate that the reduced [3Fe-4S] center can react rapidly with Fe to form a [4Fe-4S] core that must include noncysteinyl coordination (101). The carboxylate side chain of Asp 14 was proposed as the most likely candidate, since this amino acid occupies the cysteine position in the typical sequence of a 8Fe protein as indicated before. The novel [4Fe-4S] cluster with mixed S and O coordination has a midpoint redox potential of 400 mV (88). This novel coordinated state with an oxygen coordination to the iron-sulfur core is a plausible model for a [4Fe-4S] core showing unusual spin states present in complex proteins (113, 114). [Pg.377]

Protein 4.1, a globular protein, binds tightly to the tail end of spectrin, near the actin-binding site of the latter, and thus is part of a protein 4.1-spectrin-actin ternary complex. Protein 4.1 also binds to the integral proteins, glycophorins A and C, thereby attaching the ternary complex to the membrane. In addition, protein 4.1 may interact with certain membrane phospholipids, thus connecting the lipid bilayer to the cytoskeleton. [Pg.617]

Biocatalysis refers to catalysis by enzymes. The enzyme may be introduced into the reaction in a purified isolated form or as a whole-cell micro-organism. Enzymes are highly complex proteins, typically made up of 100 to 400 amino acid units. The catalytic properties of an enzyme depend on the actual sequence of amino acids, which also determines its three-dimensional structure. In this respect the location of cysteine groups is particularly important since these form stable disulfide linkages, which hold the structure in place. This three-dimensional structure, whilst not directly involved in the catalysis, plays an important role by holding the active site or sites on the enzyme in the correct orientation to act as a catalyst. Some important aspects of enzyme catalysis, relevant to green chemistry, are summarized in Table 4.3. [Pg.124]

Hemoglobin Is a large complex protein molecule the atomic model of oxyhemoglobin at 2.8 a resolution has been reported In 1968 by Perutz and coworkers, and a similar model of deoxy-hemoglobin In 1970 (1,2). The molecule Is a spheroid, approx-... [Pg.1]

C It helps to synthesize complex proteins from amino acids. [Pg.48]

Camire (2002) showed that texturization does not seem to have a great effect on mineral retention and bioavailability. Others have reported increased retention of ascorbic acid in rice- and maize-based snacks (Hazell and Johnson, 1989 Plunkett and Ainsworth, 2007), increased iron diffusibility and absorption of iron-complexed protein (Poltronieri et al, 2000 Watzke, 1998), and no difference in iron and zinc absorption in human subjects fed textured bran-flour (Fairweather-Tait et al, 1989). [Pg.188]

Serum ferritin A complex protein formed in the intestine, containing about 23% iron, the amount of ferritin found in serum is directly related to iron storage in the body. [Pg.1576]

Adenosine deaminase (ADA) is an amino hydrolase that catalyzes the deamination of adenosine and 2 -deoxyadenosine to inosine and 2 -deoxyinosine, respectively. High activity of ADA is seen in thymus and other lymphoid tissues. ADA has been shown in many different physical forms. A small form of the enzyme predominates in the spleen, stomach, and red blood cells, whereas the large form predominates in the kidney, liver, and skin fibroblasts. The small form of the catalytic subunit can be converted to the large form by complexing with a protein termed binding protein or complexing protein. [Pg.14]

Reducing complexity Protein fractionation prior to electrophoresis... [Pg.8]

Figure 2.7. Identification ofphosphoproteins by site-specific chemical modification. A. Method of Zhou et al. (2001) involves trypsin digest of complex protein mixture followed by addition of sulfhydryl groups specifically to phosphopeptides. The sulfhydryl group allows capture of the peptide on a bead. Elution of the peptides restores the phosphate and the resulting phosphopeptide is analyzed by tandem mass spectrometry. B. Method of creates a biotin tag in place of the phosphate group. The biotin tag is used for subsequent affinity purification. The purified proteins are proteolyzed and identified by mass spectrometry. Figure 2.7. Identification ofphosphoproteins by site-specific chemical modification. A. Method of Zhou et al. (2001) involves trypsin digest of complex protein mixture followed by addition of sulfhydryl groups specifically to phosphopeptides. The sulfhydryl group allows capture of the peptide on a bead. Elution of the peptides restores the phosphate and the resulting phosphopeptide is analyzed by tandem mass spectrometry. B. Method of creates a biotin tag in place of the phosphate group. The biotin tag is used for subsequent affinity purification. The purified proteins are proteolyzed and identified by mass spectrometry.
The experiments described above indicate that technology is available to couple SPR with mass spectrometry. These methods should be useful for protein-protein interaction mapping. For example, immobilized proteins can be used as hooks for fishing binding partners from complex protein mixtures under native conditions. The coupling of techniques can lead not only to the rapid identification of interacting proteins but will also provide information on the kinetic parameters of the interaction. This approach should serve as an excellent complement to the use of in vivo techniques such as the yeast two-hybrid system. [Pg.105]

Gygi, S. P., Rist, B., Gerber, S. A., Turecek, F., Gelb, M. H., and Aebersold, R. (1999). Quantitative analysis of complex protein mixtures using isotope-coded affinity tags. Nat. Biotechnol. 17, 994-999. [Pg.114]

Wright, G. L., Cazares, L. H., Leung, S.-M., Nasim, S., Adam, B.-L., Yip, T.-T., Schellhammer, P. F., Gong, L., and Vlahou, A. (2000). ProteinChip surface enhanced laser desorption/ionization (SELDI) mass spectrometry a novel protein biochip technology for detection of prostate cancer biomarkers in complex protein mixtures. Prostate Cancer and Prostatic Diseases 2, 264-276. [Pg.124]

Proteins, the main constituents of the animals body, are polypeptides, biopolymers consisting of many amino acid molecules (the monomers) combined together (see Chapter 11) collagen, for example, the main component of animal skin, is a complex protein consisting of many molecules of amino acids combined together into polypeptide chains (see Fig. 71). Polysaccharides, the essential constituents of plants, also consist of many monosaccharide molecules combined together. Cellulose, the most abundant biological material on earth, which makes up most of the structural... [Pg.339]


See other pages where Complexes protein is mentioned: [Pg.2991]    [Pg.169]    [Pg.350]    [Pg.57]    [Pg.311]    [Pg.372]    [Pg.223]    [Pg.695]    [Pg.253]    [Pg.154]    [Pg.488]    [Pg.232]    [Pg.405]    [Pg.329]    [Pg.412]    [Pg.463]    [Pg.4]    [Pg.1017]    [Pg.103]    [Pg.131]    [Pg.65]    [Pg.811]    [Pg.15]    [Pg.9]    [Pg.19]    [Pg.351]    [Pg.352]    [Pg.409]   
See also in sourсe #XX -- [ Pg.267 ]

See also in sourсe #XX -- [ Pg.61 ]




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Activating protein 1 complexes

Activator protein-1 complex

Adaptor protein complex

Affinity purification of RNA-protein complexes

Amicyanin protein complex

Apical protein complex

Aptamer protein complexes, analysis

Bacteriochlorophyll-protein complex structure

Bacteriochlorophyll-protein complexes

Binding Protein Complex eIF

Binding protein-enzyme complex

Calcium complexes proteins

Carbohydrates protein complexes

Carotenoid-protein complexes

Chitin protein complexes

Chitin-protein complex from

Chlorins protein complexes

Chlorophyll protein complex

Chlorophyll-carotenoid-protein complexe

Chloroplasts protein complexes

Chondroitin sulfate-protein complex, biosynthesis

Coactivator-complex proteins

Coagulation proteins prothrombin complex concentrate

Colloidal gold protein complexes

Complex Rieske iron sulfur protein

Complex lipids, synthesis proteins

Complex mixtures, protein components

Complex protein molecules

Complex protein-polysaccharide

Complex protein-surfactant

Complex proteomes proteins

Complex systems lipid-protein mixtures and cell membranes

Complex systems protein folding

Complexation with Proteins

Complexed protein spectra

Complexes gold-protein

Complexes protein-substrate

Complexes with proteins

Contractile protein complex

Copper coordination complexes, models proteins

Copper proteins model complexes

Copper proteins normal” complexes

Copper, complexes proteins

Cross-linked protein complexes

Crystallographic protein-ligand complexes

Cysteine-Containing Oligopeptide Model Complexes of Iron-Sulfur Proteins

Cytochrome protein—electrode complex

DNA complex with Trp repressor protein

DNA complex with zinc finger protein

DNA-protein complexes

Database ligand-protein complex

Detergent-protein complexes

Dinuclear copper proteins model complexes

DnaK, Hsp70-protein complexes

Dynamics of water around a protein-DNA complex

Dystrophin-associated protein complex

Electron-transport assemblies protein complexes

Factors influencing protein-polyelectrolyte complexes

Formation of RNA-protein complexes

Fruit juice protein complex

Functional analysis of RNA-protein complexes in vitro

G protein complex

G protein-coupled receptors complexes

Glucan mannan-protein complex

Glycans protein complexes

Glycosidic bond, protein-carbohydrate complexes

Gold-Protein Reactions and Complexes

Golgi complex protein glycosylation

Golgi complex protein modification

H-bonds in Protein-Nucleic Acid Complexes

Heme proteins model complexes

Heparin protein complex

Heparinic acid protein complex

High-Spin NO Complexes with Non-Heme Iron Proteins

High-quality ligand-protein complexes

Hormone protein complex

Hsp70-protein complexes

Hyaluronic acid complex with protein

Hyaluronic acid, complex formation with proteins

I 6 Hydrogen Bonds in Protein-Ligand Complexes

Inclusion complexes with proteins

Interaction protein complexes

Iodine complex protein effects

Iron succinyl-protein complex

Iron-protein complex

Iron-sulfur protein complex

Iron-sulfur proteins high-potential, thiolate complexes

Iron-sulfur proteins nitric oxide complexes

Kinetic Complexity of Protein Electron Transfer Reactions

Labeling of Proteins with Organometallic Complexes Strategies and Applications

Lactose-protein complexes

Ligand-protein complexes, induction

Ligand-protein complexes, induction functional

Ligand-protein complexes, induction functionals

Ligands as Wrappers of Proteins in PDB Complexes Bioinformatics Evidence

Light-harvesting complex proteins

Light-harvesting pigment protein complex

Light-harvesting pigment protein complex isolation

Light-harvesting pigment protein complex model

Light-harvesting pigment protein complex photosynthetic bacteria

Ligno-protein complexes

Lipid-Protein Complexes

Lipide-protein complex

MRNA-protein complex

Magnesium protein complex

Magnetic susceptibility, heme protein complexes

Major histocompatibility complex MHC) proteins

Major histocompatibility complex class I proteins

Major histocompatibility complex proteins

Major histocompatibility complex proteins class

Major histocompatibility complex proteins peptide presentation

Major histocompatibility complex proteins structure

Mammalian achaete-scute complex-like protein

Manganese complexes proteins

Mannan protein complex

Mannans protein complex with

Mass spectrometry metal-protein complexes

Membrane bound protein complex

Metal-complexes with Proteins

Metallo-protein complexes

Methylamine dehydrogenase protein complex

Mitochondria protein complexes

Mitochondrial lipid-protein complexes

Mixed protein gels, complex

Mn protein complex

Molecular complexes proteins

Monoclonal antibodies complexed with protein

Mucopolysaccharides mucopolysaccharide-protein complex

Nanoparticle-protein complex

Nitric Oxide Complexes of Ferrohemes in Proteins

Nitric Oxide Complexes of Iron-Sulfur Proteins

Nitric Oxide Complexes of Other Nonheme Iron Proteins

Nitric oxide complexes nonheme iron proteins

Oligosaccharide-protein complexes

Peridinin chlorophyll-protein complex

Photosynthetic pigment-protein complexes

Photosystem protein complexes

Phytate protein complex

Pigment-protein complexes

Pigment-protein complexes Photosystem

Pigment-protein complexes light-harvesting complex

Plasticity protein complexes

Poly globular protein complexation

Poly protein complexes

Polyelectrolyte complexes (polyion protein

Polyelectrolyte complexes protein carriers

Polyelectrolyte-protein complexes

Polyelectrolyte-protein complexes coacervation

Polyelectrolyte-protein complexes enzyme activity

Polyelectrolyte-protein complexes precipitation

Polyelectrolyte-protein complexes solubility

Polysaccharide-protein complexes/interactions

Potato starch complexation with proteins

Preparation of Protein A-Gold Complexes

Protein A-IgG complexes

Protein Complex Formation

Protein antigens structural complexity

Protein cavities, metal complexes

Protein complex isolated from culture

Protein complexes characteristics

Protein complexes native

Protein complexes synthetic

Protein complexes with polyelectrolytes

Protein complexes, electron transfer

Protein complexes, interfacial films

Protein complexes, nonspecific

Protein complexes, purification

Protein complexity

Protein complexity

Protein complexity evolution

Protein folding complex mechanisms

Protein folding complexity

Protein from complex mixtures

Protein kinase replication complex

Protein ligand complexes

Protein lipid complex, disadvantages

Protein multienzyme complexes

Protein nucleic acid complexes

Protein polyphenol complexes

Protein reagent complex, equilibrium

Protein supramolecular chemistry enzyme complexes

Protein tyrosine kinases signaling complexes

Protein-Small Molecule Complexes

Protein-carbohydrate complexes, computer

Protein-cellodextrin complexes

Protein-drug complex

Protein-electrolyte complexes

Protein-enzyme complexes

Protein-inhibitor complexes

Protein-inhibitor complexes, conformational

Protein-inhibitor complexes, conformational energies

Protein-ligand complexes, binding mode

Protein-ligand complexes, molecular

Protein-ligand complexes, molecular recognition

Protein-ligand docking complexes

Protein-ligand interactions/complexes

Protein-lipid respiratory chain complexes

Protein-peptide interactions/ complexes

Protein-phospholipid complex

Protein-phospholipid complex, physical

Protein-polyelectrolyte complexes, factors

Protein-saccharide complexes

Protein-small molecule interactions/ complexes

Protein-starch complexes

Protein-starch complexes characteristics

Protein-starch complexes native

Protein-starch complexes synthetic

Protein-surfactant complexation

Protein-surfactant complexes, solubilizing

Proteins ODNA) complex

Proteins SDS complexes

Proteins TCDD complex

Proteins avidin-biotin complex

Proteins carbohydrate complexes with

Proteins complexation

Proteins complexation

Proteins complexes induced

Proteins major histocompatibility complex-associated

Proteins major urinary protein complex

Proteins metal complexes

Proteins protein—ligand complexes

Proteins prothrombin complex activity

Proteins repressive complex

Proteins, complexes with heparin

Proteoglycans mucopolysaccharide-protein complexes

Proteomics protein-complex identification

Quenching probe/protein complexes

Receptor-G protein complex

Renin-protein complex

Retinol-binding protein-transthyretin complex

Ribosome protein complexes

Ruthenium complexes proteins

SIFt and the Analysis of Protein Kinase - Inhibitor Complexes

Scoring protein-ligand complexes

Separation complex protein mixture

Settlement induced protein complex

Settlement-inducing protein complex

Simple and Complex Iron-Sulfur Proteins

Simple and Complex Iron-Sulfur Proteins in Sulfate Reducing

Simple and Complex Iron-Sulfur Proteins in Sulfate Reducing Bacteria

Skpl/Cull/F-Box Protein Complex

Small Molecules in Self-Crystals and Protein-Carbohydrate Complexes

Sodium dodecyl sulfate protein complex

Spectrin-protein 4.1-actin complex

Spin NO Complexes with Non-Heme Iron Proteins

Stability constants protein complexes

Starch phosphates complexation with proteins

Steroid-protein complex

Stress-70 protein family complexes

Synaptonemal complex proteins

TATA binding protein preinitiation complex

TFIIH-A Pivotal Regulatory Protein Complex

Tannin protein complexes

Tannin-protein complexation

The Complexity of Protein Biosynthesis

The complexity of G protein signalling

Thiolate complexes, iron-sulfur proteins

Three-dimensional protein-ligand complex

Toward a Model of the Receptor-G Protein Complex

Trace metals protein complexes

Ubiquitin Domains in Complex Proteins

Ubiquitin complex proteins

Zirconium complexes proteins

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