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Dissecting the function of Atg1 complex in Dictyostelium autophagy
Dissecting the function of Atg1 complex in Dictyostelium autophagy

... generates a PtdIns3P-enriched region at the level of the endoplasmic reticulum (ER) to which the complex formed by Atg2 and Atg18/WIPI is recruited. Concomitantly, Atg12 is covalently bound to Atg5, and the Atg12–Atg5 conjugate form a ternary complex with Atg16L1, which is required for the subsequen ...
The Bacterial Phosphotransferase System: Structure, Function
The Bacterial Phosphotransferase System: Structure, Function

... molecular genetic and physiological studies of the PTS, Jonathan purified many PTS proteins to homogeneity in preparation for collaborative 3-dimensional structural analyses by both x-ray crystallography and multidimensional NMR. Preparation of mutant forms of these proteins as well as 13C and 15N d ...
Primary production of protein: I. Comparison of net cellular carbon
Primary production of protein: I. Comparison of net cellular carbon

... Radioisotopic tracers other than "C associated with distinct types of algal cell material have been used to monitor specific biochemical activities. These include 'H-adenine (Karl 1982, Winn & Karl 1984) and 32P04 (Cuhel & Waterbury 1984) to assess nucleic acid biosynthesis, and to trace the product ...
The Biologically Appropriate Food Concept
The Biologically Appropriate Food Concept

... and cats – essential to basic body functions, including cellular regeneration, tissue maintenance, hormone and enzyme production, and the provision of energy. Although protein is essential, not all proteins function equally, with protein qualities varying enormously between various sources. Three fa ...
Recombinant expression and characterisation of monofunctional S-
Recombinant expression and characterisation of monofunctional S-

... domains. The deduced amino acid sequence of the bifunctional PfAdoMetDC/ODC predicted a molecular mass of 166 kDa for the polypeptide, whereas the recombinantly expressed enzyme had a molecular mass of -330 kDa. This suggested that the enzyme consists of a heterotetrameric structure derived from two ...
Keep Your Fingers Off My DNA: Protein–Protein
Keep Your Fingers Off My DNA: Protein–Protein

... Gata1 (FOG1) and its binding partners, the globin transcription factor GATA1 and Transforming Acidic Coiledcoil 3 (TACC3). FOG1 contains a total of nine ZFs (Table 2); however, only four are of the classic C2H2 type. The remaining fingers substitute a conserved cysteine for the final histidine [36]. ...
Di-(2-ethylhexyl) phthalate mediates glycolysis and the TCA cycle
Di-(2-ethylhexyl) phthalate mediates glycolysis and the TCA cycle

... and were successfully identified . Among these proteins, 25 were successfully annotated and 3 did not yield unambiguous protein identification. Among the identified proteins, 11 were involved in glycolysis (spot 3, 4, 7, 8, 9, 11, 15, 19, 20, 21, 23), and 10 members had at least a 1.5-fold decrease ...
Nitrogen Balance With Sheep on Rations Containing Urea
Nitrogen Balance With Sheep on Rations Containing Urea

... the favorable effect of ammonium salts on the nitrogen balance of an1malI with simple stomachs, suppression of deamination of animo acids has been suggested. As applled to ruminant nutrition, the explanation that protein· Is synthesized from ammonia in the rumen and digested in the lower reg10Da of ...
(De)regulation of key enzyme steps in the shikimate pathway and
(De)regulation of key enzyme steps in the shikimate pathway and

... 7-phosphate (DAHP) synthase are key regulatory enzymes in aromatic amino acid biosynthesis in the actinomycete Amycolatopsis methanolica. Deregulated, feedback-control-resistant mutants were isolated by incubation of A. methanolica on glucose mineral agar containing the toxic analogue p-fluoro-DL-ph ...
GENETICS TEST IV - Daytona State College
GENETICS TEST IV - Daytona State College

... • A frameshift mutation occurs when any number of bases are added or deleted, except multiples of three, which would reestablish the initial frame of reading. • The triplet nature of the genetic code was revealed by frameshift mutations. • +1 base = mutant (changes all amino acids down stream from i ...
Feeney_ku_0099D_12934_DATA_1 - KU ScholarWorks
Feeney_ku_0099D_12934_DATA_1 - KU ScholarWorks

... Purpose: Oxidative post-translational modification of protein-bound tyrosine residues can have a significant impact on protein structure and function and thus may be important to physiological and pathological processes. Oxidative stress has been correlated with biological aging and many disease sta ...
Interplay of pH and Binding of Multivalent Metal Ions: Charge
Interplay of pH and Binding of Multivalent Metal Ions: Charge

... A complete model for the protein charge in any system has to include both local and nonlocal contributions, although many studies focus on only one approach.36,37 The driving force of ion-induced surface charge is the change in free energy upon ion condensation on the surface, which can be described ...
The role of multifunctional M1 metallopeptidases
The role of multifunctional M1 metallopeptidases

... Aminopeptidase N (APN), sometimes called alanyl aminopeptidase or CD13, is a heavily glycosylated protein, and plays a role in regulating blood pressure by converting the seven-amino acid AngIII to AngIV to abrogate the effects of AngIII. APN can process a number of peptide substrates including the ...
Chapter 10
Chapter 10

... into the endoplasmic reticulum where protein folding and processing take place. From the endoplasmic reticulum, proteins are transported in vesicles to the Golgi apparatus where they are further processed and sorted for transport to endosomes, lysosomes, the plasma membrane, or secretion from the ce ...
Protein 3D-structure analysis
Protein 3D-structure analysis

... http://www.rcsb.org/pdb/explore/explore.do?structureId=1THC Similar structure: 2H6U What is the function of transthyretin, respectively of other proteins with similar structure? Have a look at the corresponding UniProt entries! How are they classified at CATH Use text search http://www.cathdb.info/c ...
The Serum Proteins of the Rat During Development
The Serum Proteins of the Rat During Development

... albumin component was detected in the present work. The relative concentration of the pre-albumin listed by Gurvich & Karsaevskaya (1956) ranges from 16-00 to 21 -0 per cent., whereas the largest average value measured in the present work was 11-3±2-9 per cent. It is likely, therefore, that the pre- ...
as a PDF
as a PDF

... mutagenesis of the catalytic Cys results in an inactive phosphatase in an assay with 32Plabeled substrates (Guan and Dixon, 1991). When the invariant Asp is mutagenized, there is a marked reduction in catalytic activity (Zhang et al., 1994b) and substrates remain bound to the enzyme (Flint et al., 1 ...
Protein S-nitrosylation in photosynthetic organisms: A
Protein S-nitrosylation in photosynthetic organisms: A

... 2 accumulates due to external signals or stress conditions, nitrate reduction is inhibited and NR preferentially produces NO from nitrite [27]. Nevertheless, nitrite-dependent NO production is not strictly dependent on the activity of NR. In roots, a plasma membrane-bound nitrite/ NO reductase (Ni-N ...
AKAP MEDIATED SIGNAL TRANSDUCTION Jennifer J. Carlisle
AKAP MEDIATED SIGNAL TRANSDUCTION Jennifer J. Carlisle

... AKAP75, were originally discovered as contaminants of type II PKA holoenzyme preparations (23, 24). The family has since grown to include over 50 members. AKAPs are structurally diverse but functionally similar proteins defined on the basis of their ability to bind to PKA and coprecipitate catalytic ...
Partial Class Notes Chapter 10 Carbohydrates
Partial Class Notes Chapter 10 Carbohydrates

... • Amino sugars of glucose and galactose occur commonly in glycoconjugates ...
Amino Acids and Proteins
Amino Acids and Proteins

... arrangements (conformations) of amino acids in localized regions of a polypeptide or protein • To determine from model building which conformations would be of greatest stability, Pauling and Corey assumed that 1. all six atoms of each peptide bond lie in the same plane and in the s-trans conformati ...
Types and effects of protein variations. Vihinen
Types and effects of protein variations. Vihinen

... Variations manifest their effects at different ways. Of the identified disease-causing cases large proportion appears in protein coding DNA and RNA sequences, although the proteincoding regions constitute only about 1.3 % of human genome. Due to the large number of different functions in which prote ...
Cellular uptake of fatty acids driven by the ER-localized acyl
Cellular uptake of fatty acids driven by the ER-localized acyl

Lecture 27
Lecture 27

... glycolytic intermediate 3phosphoglycerate to serine. 1. Conversion of 3phosphoglycerate’s 2-OH group to a ketone 2. Transamination of 3phosphohydroxypyruvate to 3-phosphoserine 3. Hydrolysis of phosphoserine to make ...
Structural Influences: Cholesterol, Drug, and Proton Binding to Full
Structural Influences: Cholesterol, Drug, and Proton Binding to Full

... observed cross peaks would be dominated by magnetization transfer within the conductance domain. In addition, the only ambiguities for Ala29 and Ala30 residues in the TM helix are two Ala residues in the C-terminus where there is a single Ile residue (Ile94). This Ile residue is directly involved in ...
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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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