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PCtpc201500393rar1_pap_plantcell 1..22
PCtpc201500393rar1_pap_plantcell 1..22

... (A) Position of the ALIX locus on chromosome 1 of Arabidopsis (BAC F9L1). The sequence surrounding the alix-1 mutation (G-to-A transition), as well as the resulting amino acid change (Gly260-to-Asp), is shown. The exon structure of ALIX is represented with boxes (light, untranslated; dark, coding re ...
Get PDF - Wiley Online Library
Get PDF - Wiley Online Library

... metabolite changes in pastes of soybeans and soybean–maize blends was studied. Pastes composed of 100% soybeans, 90% soybeans and 10% maize, and 75% soybeans and 25% maize were naturally fermented (NFP), and were fermented by lactic acid bacteria (LFP). LAB fermentation processes were facilitated th ...
as a PDF - CiteSeerX
as a PDF - CiteSeerX

... intercellular interactions. The extracellular domain of CD34 shares structural similarity with another sialomucin, CD43, a hematopoietic cell-specific protein implicated in cell-cell adhesion, tyrosine kinase activation, and cytoskeletal interactions.4 Like CD43, CD34 ...
From Sequence to Structure
From Sequence to Structure

... peptide backbone, to polar organic molecules, and to water. This tendency dominates the interactions in which they participate. Some of them can change their charge state depending on their pH or the microenvironment. Aspartic acid and glutamic acid have pKa values near 5 in aqueous solution, so the ...
Architecture and Biosynthesis of the Saccharomyces cerevisiae Cell
Architecture and Biosynthesis of the Saccharomyces cerevisiae Cell

... participate in wall construction as hydrolases or transglycosidases. The second contains nonenzymatic agglutinins, flocculins, or b1,3-glucan cross-connectors (Klis et al. 2006, 2010; Dranginis et al. 2007; Goossens and Willaert ...
Turnover of protein phosphorylation evolving under
Turnover of protein phosphorylation evolving under

... with its SH2 domain, which closes the kinase into an inactive conformation (Frame, 2002). Because single phosphorylation sites in specific cases play key roles in protein regulation, mutations at these sites may have complex organismal phenotypes. For instance, mutation of Ser47 on the Drosophila cir ...
Isolation of Rat Transferrin Using CNBr-Activated
Isolation of Rat Transferrin Using CNBr-Activated

... iron containing proteins transferrin and ferritin in a homogeneous state. Transferrin is the most important transport protein in serum due to its quantity and biological role in the transport of iron to the haemopoietic system. For experimental work on model systems in animals we need purified trans ...
How proteins produce cellular membrane curvature
How proteins produce cellular membrane curvature

... elasticity is characterized by the elastic moduli, such as the bending moduli of the membrane monolayer, κm, and bilayer, κB, the moduli of the Gaussian curvature of the monolayer and bilayer, κ m and κ B , respectively, the membrane stretching modulus, Г (see Supplementary information S1 (box) and ...
Protein stabilization: a common consequence of mutations
Protein stabilization: a common consequence of mutations

... in association with its obligate partner, Max. Both dimerization with Max through the C-terminal helix ± loop ± helix/leucine zipper (HLH-LZ) domain and sequence-speci®c DNA binding mediated by the adjacent basic region (B) are prerequisites for Myc to function, and the resulting Myc : Max complex t ...
as a PDF
as a PDF

... Sugar fermentation was long considered the sole means of energy metabolism available to lactic acid bacteria. We recently showed that metabolism of Lactococcus lactis shifts progressively from fermentation to respiration during growth when oxygen and heme are available. To provide insights into this ...
Role of Protein Carbonylation in Skeletal Muscle Mass Loss
Role of Protein Carbonylation in Skeletal Muscle Mass Loss

... of proteins induced by reactive nitrogen species (RNS). Oxidative stress-induced cellular damage in tissues can be identified using different methodologies. For instance, carbonyl-modified proteins are commonly detected using hydrazide, which reacts specifically with protein carbonyls in the form of ...
HIBERNATING BEARS, ANTIBIOTICS AND THE EVOLVING RIBOSOME
HIBERNATING BEARS, ANTIBIOTICS AND THE EVOLVING RIBOSOME

... Proteins are constantly being degraded. Therefore simultaneous production of proteins is required. The translation of the genetic code into proteins is performed by a complex apparatus comprising the ribosome, messenger RNA (mRNA), transfer RNAs (tRNAs) and accessory protein factors. The ribosome, a ...
27. biosynthesis of amino acids
27. biosynthesis of amino acids

... intermediates as precursors. Fig 27-2 (on the next page) highlights the relationship between amino acid metabolism and the citric acid cycle intermediates. Essential and Nonessential Amino Acids The organisms differ markedly in terms of their ability to carry out the de novo synthesis of the protein ...
Proteases - Home - KSU Faculty Member websites
Proteases - Home - KSU Faculty Member websites

... • Unlimited proteolysis: in which proteins are degraded into their amino acid constituents. – Ubiquitin/proteasome pathway: First conjugated to multiple molecule of the polypeptide ubiquitin. This modification marks them for rapid hydrolysis by the proteasome in the presence of ATP. – Lysosome pathw ...
TY10618.CHP:Corel VENTURA
TY10618.CHP:Corel VENTURA

... stored at 4°C and subsequently used within 3 days. The stimulus concentration at the target was estimated, by measuring liquid junction potentials, to be diluted by at least a factor of 10 compared with the concentration in the stimulating pipette liquid. Therefore, the actual concentrations for ami ...
Brown, V, Small, K, Lakkis, L, Feng, Y, Gunter, C, Wilkinson, KD and Warren, ST: Purified recombinant Fmrp exhibits selective RNA-binding as an intrinsic property of the fragile X mental retardation protein. Journal of Biological Chemistry 273:15521-15527 (1998).
Brown, V, Small, K, Lakkis, L, Feng, Y, Gunter, C, Wilkinson, KD and Warren, ST: Purified recombinant Fmrp exhibits selective RNA-binding as an intrinsic property of the fragile X mental retardation protein. Journal of Biological Chemistry 273:15521-15527 (1998).

... Fmrp Constructs—The baculoviral constructs used in wild type Fmrp production were constructed by inserting the sequence GACTACAAGGACGACGATGACAAG encoding the FLAG epitope into full-length fmr1 cDNA between the second and third amino acids. The fmr1 Mc2.17 cDNA (18) includes 123 bases upstream of the ...
Structure of the ordered hydration of amino acids
Structure of the ordered hydration of amino acids

Structural and Functional Studies on Proteinaceous Metallocarboxypeptidase Inhibitors  Joan López Arolas
Structural and Functional Studies on Proteinaceous Metallocarboxypeptidase Inhibitors Joan López Arolas

... Proteolytic enzymes, also known as peptidases or proteases*, catalyze the hydrolytic cleavage of peptide bonds in other proteins. Some peptidases are involved in intra- and extra-cellular protein digestion, but most of them perform much more specialized tasks such as activation of zymogens, processi ...
Chapter 2
Chapter 2

... The first stage of the screening procedure for commercial enzymes is to screen ideas, i.e. to determine the potential commercial need for a new enzyme, to estimate the size of the market and to decide, approximately, how much potential users of the enzyme will be able to afford to pay for it. In som ...
PDF
PDF

... (Mr 27-5 x 103, component of band 5 on ID), 32 (Mr 27-5 x 103, component of band 5 on ID), 33 (Mr 25-5 x 103, band 3 on ID) and 34 (Mr 11-5 x 103). By contrast, although several of the major proteins synthesized by the oocyte before maturation become prominent during maturation e.g. polypeptides 14 ...
Quantum binding energy features of the T3-785
Quantum binding energy features of the T3-785

... of human type III collagen) and C-terminal (four Pro–Hyp–Gly triplets). Its Fig. ES5‡ depicts also the subsystems AB (A chain interacting with the B chain), BC (B chain interacting with the C chain) and CA (C chain interacting with the A chain). Despite its simplied sequence and regular structure, ...
The Metamorphosis of the Aleurone Protein Storage Vacuole
The Metamorphosis of the Aleurone Protein Storage Vacuole

... about how GA and ABA affect the transcription of genes for abundantly transcribed enzymes such as α-amylase. GAand ABA-responsive elements have been identified in the promoters of several cereal aleurone genes, and functional trans-acting factors have been found (Jacobsen et al., 1995). Much less is ...
Rapid Reversion from Monomer to Dimer
Rapid Reversion from Monomer to Dimer

... novo synthesis following destruction of the monomer. Rather, regeneration occurs by reversion from the monomer to the dimer. However, regeneration of dimeric UVR8 in darkness following UV-B exposure occurs much more rapidly in vivo than in vitro with illuminated plant extracts or purified UVR8, indic ...
The SMN Complex Is Associated with snRNPs throughout Their
The SMN Complex Is Associated with snRNPs throughout Their

... The common neurodegenerative disease spinal muscular atrophy is caused by reduced levels of the survival of motor neurons (SMN) protein. SMN associates with several proteins (Gemin2 to Gemin6) to form a large complex which is found both in the cytoplasm and in the nucleus. The SMN complex functions ...
26. oxidation of amino acids
26. oxidation of amino acids

... compound before export from extrahepatic tissues into the blood and thence to the liver or kidneys. This transport function is accomplished by L-glutamine and not by glutamate which is so critical to amino group metabolism. In many tissues, ammonia enzymatically combines with glutamate to yield glut ...
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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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