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Molecular analysis of Physarum haemagglutinin I
Molecular analysis of Physarum haemagglutinin I

... The slime mould is a suitable organism for the study of cell growth and development at the biochemical and molecular levels. It has been reported that the expression of numerous genes is regulated during the Physarum life cycle (Schreckenbach & Werenskiold, 1986). The expression of haemagglutinins i ...
Processing of the Presequence of the Schizosaccharomyces pombe
Processing of the Presequence of the Schizosaccharomyces pombe

... S. pombe Iron-Sulfur Protein Is Processed in One Step When Imported into S. pombe or S. cerevisiae Mitochondria—Mitochondrial precursor proteins that are cleaved in two sequential steps by MPP and MIP share a highly conserved three amino acid motif RX(2)(F/L/I)XX(T/S/G)XXXX(2) at the carboxyl termin ...
Similarities and Differences in the Glycosylation Mechanisms in
Similarities and Differences in the Glycosylation Mechanisms in

... numbering about 12 in archaea, 14 in yeast, and up to 19 in mammals. Bacteria also have a polyisoprene as their LLO lipid but, instead of dolichol, they use undecaprenol (11 isoprene units) which has one more double bond than the same length dolichol. This double bond is located between carbons 2 an ...
Subcellular Trafficking of Mammalian Lysosomal Proteins: An
Subcellular Trafficking of Mammalian Lysosomal Proteins: An

... Sections 2.2.2 and 2.2.3. Hence, it appears that, while atypical dileucine signals can contribute to the lysosomal sorting of some proteins, additional trafficking information may be required for their efficient sorting to the lysosomes. The transport of G-protein coupled receptor 143 (GPR143 or OA1 ...
Differential Accumulation Pattern of Met-rich beta
Differential Accumulation Pattern of Met-rich beta

... callus after 6-weeks and they are regenerated into plantlets ...
Enzyme Mechanisms
Enzyme Mechanisms

... Internal behavior of cells modulated by external influences Extracellular signals are called first messengers 7-helical transmembrane proteins with characteristic receptor sites on extracellular side are common, but they’re not the only receptors 09/30/08 Biochemistry:Transport; Nucleic Acids ...
Acquisition, Conservation, and Loss of Dual
Acquisition, Conservation, and Loss of Dual

... contain two signals, which results in the same protein being imported into two distinct locations. To date, 72 proteins in Arabidopsis have been shown to be dual targeted (Carrie et al., 2009a; Carrie and Small, 2013); however, as many as 500 are predicted to be dual targeted because they contain am ...
REDESIGN OF CARNITINE ACETYLTRANSFERASE SPECIFICITY BY PROTEIN ENGINEERING UNIVERSIDAD DE BARCELONA
REDESIGN OF CARNITINE ACETYLTRANSFERASE SPECIFICITY BY PROTEIN ENGINEERING UNIVERSIDAD DE BARCELONA

... candidate, because its side chain is voluminous and projects into the putative cavity where the acyl-CoA may enter. Our bioinformatic approach failed to identify Met564; in our protein alignment we compared all the known sequences of the carnitine/choline acyltransferase family from several organism ...
ELECTROPHORESIS SECTION OBJECTIVES : At the end of the
ELECTROPHORESIS SECTION OBJECTIVES : At the end of the

... identify the different hemoglobins and their order of migration in alkaline pH buffer and in acid pH buffer electrophoresis (cellulose acetate and agarose gel support – Helena procedure), also in capillary electrophoresis; 8. relate the different hemoglobins to the disease states; 9. list the fracti ...
ENS’06 FUSION PHAGE AS A BIOSELECTIVE NANOMATERIAL: EVOLUTION OF THE CONCEPT
ENS’06 FUSION PHAGE AS A BIOSELECTIVE NANOMATERIAL: EVOLUTION OF THE CONCEPT

... peptides fused to the major coat protein pVIII [8]. These constructs display the guest peptide on every pVIII subunit increasing the virion’s total mass by 10%. Despite of the extra burden, such particles could retain their infectivity and progeny-forming ability. There is a fast growing interest to ...
Phosphorylation of apoproteins in VLDL, and LDL by protein
Phosphorylation of apoproteins in VLDL, and LDL by protein

... structuraJ framework for the partxle with alternating hydrophilic and hydrophobic domains that interface with the aqueous medium and the lipid core of the parr.de, respectively [3). Apo BlOO also forms the receptor recognition site in LDL particles since these have lost apoE during their formation f ...
Thermo Scientific Solutions for Quantitative
Thermo Scientific Solutions for Quantitative

... exclusively qualitative technique into one that spans a continuum of qualitative and quantitative approaches. Traditionally, quantitative measurements of protein abundance were done by Western blotting. However, Western blotting almost always requires a priori knowledge of the system and the expecte ...
Immunoblot Detection of Proteins That Contain Cysteine
Immunoblot Detection of Proteins That Contain Cysteine

... GAPDH (Fig. 4–2A). The antibodies to the sulfonylated GAPDH peptides also detected GAPDH only in the H2O2treated cells—not in the nontreated cells (Fig. 4–2B). The antibodies prepared with the sulfonylated Prx VI peptide showed similar specificity for oxidized Prx VI both in recombinant proteins and ...
GFP is the way to glow: bioimaging of the plant endomembrane
GFP is the way to glow: bioimaging of the plant endomembrane

... include the soluble proteins such as sp-GFP-HDEL (Fig. 2d,f ) and colour variants (sp-YFP-HDEL; Irons et al., 2003), domains of calreticulin (Brandizzi et al., 2003), BiP (Lee et al., 2002) and the membrane protein calnexin (Irons et al., 2003), the dilysine motif GFP-tm-KKXX (Benghezal et al., 2000 ...
Heterotrimeric G proteins in C. elegans
Heterotrimeric G proteins in C. elegans

... stimulates an exchange of GTP for GDP resulting in the active signaling molecules Gα-GTP and free Gβγ, either of which can interact with effectors. Hydrolysis of GTP restores Gα-GDP, which then reassociates with Gβγ and receptor to terminate signaling. The rate of G protein activation can be enhance ...
TEXT F.H.C crick postulated the existence of “genetic code” the set
TEXT F.H.C crick postulated the existence of “genetic code” the set

... nucleotide. Accordingly a codon dictionary has been prepared and relationship of some 61 codons has been established to certain specific amino acids. The remaining three codons, UAA (also called ochre), UAG (also called amber) and UGA (also called opal) do not code for specific amino acids and befor ...
Nutrition to Support Recovery from Endurance Exercise: Optimal
Nutrition to Support Recovery from Endurance Exercise: Optimal

... Dietary carbohydrate and protein are important macronutrients for the endurance athlete, as they provide the requisite substrates to enhance glycogen resynthesis and muscle remodeling. While other aspects of recovery such as fluid restoration and/or maintenance of immune function are important consi ...
Yeast Extract
Yeast Extract

... depends on the type of yeast and to what extent the proteins have to be broken down • Separation of the insoluble part such as Yeast Cell Walls from the water soluble components of yeast (mainly proteins, peptides, amino-acids, etc...) which constitute the Yeast Extract • Concentration and pasteuris ...
Crystal structure of mouse coronavirus receptor
Crystal structure of mouse coronavirus receptor

... cleaved into a receptor-binding subunit S1 and a membranefusion subunit S2 that associate together through noncovalent interactions (Fig. 1A). S1 sequences are relatively well conserved within each coronavirus group, but differ markedly between different groups. S1 contains two independent domains, ...
galactose specific
galactose specific

... Legume lectins: peanut lectin, winged bean basic and acidic lectins and their complexes • Multimeric proteins can assume open quaternary structures • High variability in quaternary structure while the tertiary structure is essentially same • Water bridges as a strategy for generating ligand specifi ...
University of Groningen Cross-linking of dimeric CitS and GltS
University of Groningen Cross-linking of dimeric CitS and GltS

... monomers in the dimeric structure was studied by site-specific tagging of the monomers with the 10 kDa Biotin Acceptor Domain (BAD) of the oxaloacetate decarboxylase of Klebsiella pneumoniae (Bott 1997) followed by cross-linking with glutaraldehyde. The approach takes advantage of the observation tha ...
BI25M1
BI25M1

... In contrast, those C atoms that flow to acetyl CoA or acetoacetate [filled arrows in the diagram], can flow to fatty acids and (other) ketone ...
Troubleshooting SDS-PAGE-0410
Troubleshooting SDS-PAGE-0410

... Problem: Weak of missing protein bands The protein/antigen quantity Increase the sample concentration. is below the detection level of Use a more sensitive stain. the stain The proteins are not fixed in Use a stain which will fix the proteins. the gel Use a gel fixing solution. Proteins have ran off ...
Immersive Projection for Biochemical Pattern Matching
Immersive Projection for Biochemical Pattern Matching

... Proteins are large organic compounds made up of amino acids. The latter are small molecules which have a central alpha carbon (Cα) linked to an amino group (NH2), carboxyl group (COOH), a hydrogen atom and a side chain (R group), as shown in Figure 1 (a). The naturally occurring 20 different amino a ...
Metabolic Pathway Flux Enhancement by Synthetic
Metabolic Pathway Flux Enhancement by Synthetic

... predictable control over gene expression (Pfleger et al., 2006; Salis et al., 2009; Win and Smolke, 2007), and directed evolution approaches for improved enzyme characteristics (Dougherty and Arnold, 2009; Zhang et al., 2008). In this chapter, we focus on ongoing efforts to improve pathway efficienc ...
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Protein



Proteins (/ˈproʊˌtiːnz/ or /ˈproʊti.ɨnz/) are large biomolecules, or macromolecules, consisting of one or more long chains of amino acid residues. Proteins perform a vast array of functions within living organisms, including catalyzing metabolic reactions, DNA replication, responding to stimuli, and transporting molecules from one location to another. Proteins differ from one another primarily in their sequence of amino acids, which is dictated by the nucleotide sequence of their genes, and which usually results in protein folding into a specific three-dimensional structure that determines its activity.A linear chain of amino acid residues is called a polypeptide. A protein contains at least one long polypeptide. Short polypeptides, containing less than about 20-30 residues, are rarely considered to be proteins and are commonly called peptides, or sometimes oligopeptides. The individual amino acid residues are bonded together by peptide bonds and adjacent amino acid residues. The sequence of amino acid residues in a protein is defined by the sequence of a gene, which is encoded in the genetic code. In general, the genetic code specifies 20 standard amino acids; however, in certain organisms the genetic code can include selenocysteine and—in certain archaea—pyrrolysine. Shortly after or even during synthesis, the residues in a protein are often chemically modified by posttranslational modification, which alters the physical and chemical properties, folding, stability, activity, and ultimately, the function of the proteins. Sometimes proteins have non-peptide groups attached, which can be called prosthetic groups or cofactors. Proteins can also work together to achieve a particular function, and they often associate to form stable protein complexes.Once formed, proteins only exist for a certain period of time and are then degraded and recycled by the cell's machinery through the process of protein turnover. A protein's lifespan is measured in terms of its half-life and covers a wide range. They can exist for minutes or years with an average lifespan of 1–2 days in mammalian cells. Abnormal and or misfolded proteins are degraded more rapidly either due to being targeted for destruction or due to being unstable.Like other biological macromolecules such as polysaccharides and nucleic acids, proteins are essential parts of organisms and participate in virtually every process within cells. Many proteins are enzymes that catalyze biochemical reactions and are vital to metabolism. Proteins also have structural or mechanical functions, such as actin and myosin in muscle and the proteins in the cytoskeleton, which form a system of scaffolding that maintains cell shape. Other proteins are important in cell signaling, immune responses, cell adhesion, and the cell cycle. Proteins are also necessary in animals' diets, since animals cannot synthesize all the amino acids they need and must obtain essential amino acids from food. Through the process of digestion, animals break down ingested protein into free amino acids that are then used in metabolism.Proteins may be purified from other cellular components using a variety of techniques such as ultracentrifugation, precipitation, electrophoresis, and chromatography; the advent of genetic engineering has made possible a number of methods to facilitate purification. Methods commonly used to study protein structure and function include immunohistochemistry, site-directed mutagenesis, X-ray crystallography, nuclear magnetic resonance and mass spectrometry.
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