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Secreted Hepatitis B Surface Antigen Polypeptides Are Derived from
Secreted Hepatitis B Surface Antigen Polypeptides Are Derived from

... protease-sensitive transmembrane form (labeled F ) is seen after a 40-min labeling period (Fig. 2 A, lane 8); this is generated from cleavage of chains synthesized at the end of the labeling period before sufficient time has elapsed for conversion to the protease-resistant form. These studies sugges ...
Lab 5: Proteins and the small molecules that love them
Lab 5: Proteins and the small molecules that love them

... catalyze chemical reactions – increase the rate of a chemical reaction without being consumed themselves: DNA Polymerase, RNA polymerase, and the Ribosome. Many other cellular chemical reactions are also dependent upon enzymes. The breakdown of proteins, lipids, and carbohydrates ingested as food ar ...
Cardiac O-GlcNAc signaling is increased in hypertrophy and heart
Cardiac O-GlcNAc signaling is increased in hypertrophy and heart

... ventricular tissue from aortic stenosis (AS) patients and rat models of hypertension, myocardial infarction (MI), and aortic banding (AB), with and without failure. We show here that global O-GlcNAcylation was increased by 65% in AS patients, by 47% in hypertensive rats, by 81 and 58% post-AB, and 3 ...
How do bacteria respond to their environment?
How do bacteria respond to their environment?

... to nitrogen deprivation Stringent response • Make less ribosomal protein • Make less ribosomal RNA • Make less transfer RNA ...
notes - local.brookings.k12.sd.us
notes - local.brookings.k12.sd.us

... describe and give examples of chemical reactions required to sustain life (hydrolysis, dehydration synthesis, photosynthesis, cellular respiration, ADP/ATP, role of ...
Determination of Protein Molecular Weight
Determination of Protein Molecular Weight

... Background Information Determination of Protein Molecular Weight ...
Separation and Purification of Angiotensin Converting Enzyme
Separation and Purification of Angiotensin Converting Enzyme

Limits of adaptation to high dietary protein intakes
Limits of adaptation to high dietary protein intakes

... might be satis®ed: intake of preformed amino acids from the diet mainly in the form of protein, amino acids derived from protein degradation within the body and the endogenous formation of amino acids as a consequence of the individual's metabolic activity. It is now necessary to add a fourth route ...
Protein dynamics and proteolysis in plant vacuoles
Protein dynamics and proteolysis in plant vacuoles

... Plant cells cannot live without their vacuoles. The tissues and organs of a plant contain a wide variety of differentiated and specialized vacuoles—even a single plant cell can possess two or more types of vacuoles. Vacuolar proteins are encoded by nuclear genes and synthesized in the cytoplasm. The ...
H 2 O Reabsorption
H 2 O Reabsorption

... – Small plasma proteins reabsorbed in PCT – Some urea and uric acid Na+ is actively reabsorbed: First – simple diffusion: Then – 1o active transport: ...
Amino acid sequence and structural repeats in schistosome
Amino acid sequence and structural repeats in schistosome

Metabolic Incorporation of Stable Isotope Labels into Glycans
Metabolic Incorporation of Stable Isotope Labels into Glycans

... Glycosylation is one of the most common post-translational protein modifications in eukaryotic systems.1-3 It has been estimated that 60-90% of all mammalian proteins are glycosylated at some point during their existence1,3 and virtually all membrane and secreted proteins are glycosylated.2 Glycopro ...
Gene Section STK4 (serine/threonine kinase 4) Atlas of Genetics and Cytogenetics
Gene Section STK4 (serine/threonine kinase 4) Atlas of Genetics and Cytogenetics

... STK4 homodimerizes through a C-terminal motif, and removal of the C terminus results in marked activation of the kinase. STK4 is cleaved by caspases during apotosis, releasing an active 34 kD kinase fragment. STK4 associates with the WW-domain protein Salvadore, which may link STK4 to the LATS tumor ...
Higher Expression Level and Lower Toxicity of Genetically Spliced
Higher Expression Level and Lower Toxicity of Genetically Spliced

... animals. Nonstructural protein 4 (NSP4) is responsible for the enterotoxic activity of these viruses in the villus epithelial cells. Amino acids 114-135 of NSP4 are known to form the diarrhea-inducing region of this viral enterotoxin. Therefore, developing an NSP4 lacking the enterotoxin domain coul ...
Post-Translational Processing (7.1)
Post-Translational Processing (7.1)

... (determined by sequencing, biochemistry, X-ray crystallography) ...
Jürgen Sühnel 3D Structures of Biological Macromolecules
Jürgen Sühnel 3D Structures of Biological Macromolecules

... similarities, aligning sequences with structures, modeling of rigid body shifts, distortions, loops and side chains, as well as detecting errors in a model. Despite these problems, it is currently possible to model with useful accuracy significant parts of approximately one third of all known protei ...
PPT
PPT

... similarities, aligning sequences with structures, modeling of rigid body shifts, distortions, loops and side chains, as well as detecting errors in a model. Despite these problems, it is currently possible to model with useful accuracy significant parts of approximately one third of all known protei ...
Mechanisms of amino acid sensing in mTOR signaling pathway
Mechanisms of amino acid sensing in mTOR signaling pathway

... must be recognized at the plasma membrane or within an associated vacuole. Different group, however, reported that only after over 1 hour treatment of the Leu8-MAP could phosphorylate S6 in some degree and moreover, in rat adipocytes, S6K1 and 4EBP1 phosphorylation was unresponsive to Leu8-MAP or IV ...
Why nature chose phosphate to modify proteins
Why nature chose phosphate to modify proteins

... (Westheimer 1987 Science 235, 1173 – 1178). Following the fixation of the genetic code, another use for phosphate ester modification was found, namely reversible phosphorylation of the three hydroxyamino acids, serine, threonine and tyrosine, in proteins. During the course of evolution, phosphorylat ...
Protease Activity of a 90-kDa Protein Isolated from Scallop Shells
Protease Activity of a 90-kDa Protein Isolated from Scallop Shells

... The high molecular weight fractions (fraction 9–13) showing higher enzyme activity were pooled and subjected to DEAE-cellulose column chromatography for protease isolation. The bound proteins were eluted using a linear concentration gradient of NaCl (0–0.6 M) in 20 mM Tris-HCl (pH 7.5) (Figure 1B). ...
The Abundance of Cell Cycle Regulatory Protein Cdc4p Is
The Abundance of Cell Cycle Regulatory Protein Cdc4p Is

... Posttranslational modification of a protein by ubiquitin usually results in rapid degradation of the ubiquitinated protein by the proteasome. The transfer of ubiquitin to substrate is a multistep process. Cdc4p is a component of a ubiquitin ligase that tethers the ubiquitin-conjugating enzyme Cdc34p ...
Agrobacterium tumefaciens and A. rhizogenes use different proteins
Agrobacterium tumefaciens and A. rhizogenes use different proteins

... 2001) contain C-terminal signals for translocation into plant cells mediated by the VirB/D4 type IV secretion system (Fig. 1). VirE2 contains two NLSs (Citovsky et al., 1992; Zupan et al., 1996), whereas GALLS-FL contains a single bipartite NLS (Fig. 1) (Hodges et al., 2004), which is important for ...
Immunolocalization of maize transglutaminase and its substrates in
Immunolocalization of maize transglutaminase and its substrates in

... The increase of TGase with chloroplast differentiation and its specific detection in the thylakoid appressed grana indicated that this enzyme might be related to the LHCII proteins of the antenna complex, which are localized in the same grana structures [12]. The 58 kDa band present in the lightexpo ...
MND Australia International Research Update December 2016
MND Australia International Research Update December 2016

... gene were the first to be identified in people with MND. These mutations cause the SOD1 protein to be unstable and form aggregates – protein clumps – in MNs. It’s important for cells to be able to remove unstable SOD1 molecules, but in people with SOD1 mutations their MNs become unable to properly e ...
Mitochondrial stress causes increased succination of proteins in
Mitochondrial stress causes increased succination of proteins in

... 20 % of the glycolytic enzyme GAPDH (glyceraldehyde-3phosphate dehydrogenase) is succinated in skeletal muscle, consistent with a ∼ 25 % decrease in specific activity of the enzyme in this tissue. Of the four cysteine residues per subunit of GAPDH, only two (Cys149 and Cys244 ) reacted measurably wi ...
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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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