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Regents Biology
Regents Biology

... Immune System Antibodies bind to specific foreign particles, such as viruses and bacteria, to help protect the body. ...
H 3 O +
H 3 O +

... – His has a side chain pKa of 6.0 and is only 10% protonated at pH 7 – Because His has a pKa near neutral, it plays important roles as a proton donor or acceptor in many enzymes. – His containing peptides are important biological buffers ...
Immunoglobulin Heavy Chain and Binding Protein Complexes Are
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... Secretion of Ig did not appear to be an artifact of fusion, because only assembled Ig molecules were secreted, and no heavy chains were secreted from the Ag8(8) cells that were fused to Ag8.653 (Ig-) cells. To more closely examine secretion of Ig, Ag8(8) cells were prelabeled, fused, and then recult ...
MB-JASS 2007 – Session III – Properties of Channels Formed by
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... proteins. These include the binary toxins Vip1 and Vip2 with coleopteran specificity and Vip3 exhibiting lepidopteran specificity (Warren 1997; Estruch et al, 1997; Lee et al, 2003). Vip-toxins, so called because of their production during vegetative growth phase extent their insecticidal properties ...
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HICA by the Labrada Research Team HICA
HICA by the Labrada Research Team HICA

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Although the administration of testosterone clearly causes marked
Although the administration of testosterone clearly causes marked

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pdf format - Faculty members Homepages
pdf format - Faculty members Homepages

... One encodes a protein that is 1,011 aa long. The other encodes a protein 879 aa long. Database analyses of these cDNAs against human genomic DNA sequences indicate that these two cDNAs are generated by alternative splicing (Fig. 1B). The HDAC9 cDNA sequences from the known 5⬘ end of HDRP cDNA to the ...


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Insulin-Containing Amino Acids and Oligopeptides/β

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Free Sample - Buy Test banks and Solution Manuals
Free Sample - Buy Test banks and Solution Manuals

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... with ClaI and EcoRI restriction enzymes and cloned into the DDK/pMBLNSS208 vector in the identical sites to yield the constructs in Figs. 2D and 2E. Transformation of P. pastoris The plasmid constructs were digested with SacI and transformed into the P. pastoris (his−) strain. Transformation was car ...
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2.3.3 Protein and amino acid metabolism

... transporters. Nevertheless, it is apparent that the combination of a multitude of transporters with overlapping specificity and differing energetics, as well as facilitation of both uptake and exchange, makes the physiological interpretation of the roles of these transporters challenging. These amin ...
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Evolution by leaps: gene duplication in bacteria | SpringerLink

The Ubiquitin System for Protein Degradation and Some of Its Roles
The Ubiquitin System for Protein Degradation and Some of Its Roles

... learned from Mager in the purification of enzymes of purine nucleotide metabolism from erythrocytes. Hemoglobin constitutes about 80–90 % of the total protein of erythrocytes and reticulocytes, and therefore the first task in the purification of any enzyme from these cells is to get rid of the great ...
Peptide Formulation: Challenges and Strategies
Peptide Formulation: Challenges and Strategies

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m5zn_a9c640ccbe96115

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Ch 16.4 Enzymes and rest

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... • Amino acids consist of four components attached to a central carbon, the alpha carbon. • These components include a hydrogen atom, a carboxyl group, an amino group, and a variable R group (or side chain). – Differences in R groups produce the 20 different amino acids. Copyright © 2002 Pearson Educ ...
Polyamines Regulate Growth Factor
Polyamines Regulate Growth Factor

... membrane was washed thoroughly to remove unspecifically bound antibodies for 5 min each, two times with only basic blot buffer, and once with basic blot buffer with 0.25% NP-40. Proteins were detected by an enhanced chemiluminescence reagent using a commercial ECL kit (Amersham, Arlington Heights, I ...
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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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