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Identifying Macronutrients - School Nutrition and Fitness
Identifying Macronutrients - School Nutrition and Fitness

... Lentils Some Fruits • Banana • Plantain ...
CH 908: Mass Spectrometry Lecture 9 Electron Capture Dissociation
CH 908: Mass Spectrometry Lecture 9 Electron Capture Dissociation

... Fundamental points about conformational studies • While exciting, these are often very difficult experiments, requiring a lot of time and good control experiments • The data one gets is often ambiguous, but no more so than solid state structures obtained in X-Ray crystallography • It’s crucial to d ...
Complete genomic sequence of viral hemorrhagic septicemia virus
Complete genomic sequence of viral hemorrhagic septicemia virus

... compartiments of virus infected cells. In the VHSV and IHNV genomes, an additional second ORF contained in the P gene is also present. The deduced hypothetical 46 and 42 amino acid proteins also exhibit basic properties and are arginine rich as described for VSV. The isoelectric points of this addit ...
Molecular cloning and computational characterization of thymidylate
Molecular cloning and computational characterization of thymidylate

... interaction of amino acid of WSSV TS. Extinction coefficients are in units of M‐1 cm‐1, at 280 nm measured in water. The initial value was assumed 44,140 by all pairs of Cys residues whereas 43890 assuming all Cys residues are reduced in another calculated by ProtParam shown that all cystine residue ...
B1 - BBS Biology Revision
B1 - BBS Biology Revision

... a) Protein molecules are made up of long chains of amino acids. These long chains are folded to produce a specific shape that enables other molecules to fit into the protein. Proteins act as: ■ structural components of tissues such as muscles ■ hormones, ■ antibodies ■ catalysts. b) Catalysts increa ...
TG-ProteinPartners-ver8 - RI
TG-ProteinPartners-ver8 - RI

... attractions can form. In addition, the areas of charge line up opposite to each other — wherever there is a positive area on the protein, the corresponding part of the partner is negative and vice versa. (The observant student may note that a neutral area is also matched on the partner.) Small molec ...
Homology Modeling Tutorial
Homology Modeling Tutorial

... (Expected value): closer to zero higher level of sequence similarity. The quality of the homology model is dependent on the quality of the sequence alignment and template structure. The approach can be complicated by the presence of alignment gaps (commonly called indels) that indicate a structural ...
Biol 115 DNA, the Thread of Life
Biol 115 DNA, the Thread of Life

... The amino acids specified by each mRNA codon. Multiple codons can code for the same amino acid. The codons are written 5' to 3', as they appear in the mRNA. AUG is an initiation codon; UAA, UAG, and UGA are termination (stop) codons. Biol115_2014_Lecture 7 ...
Proteins
Proteins

... If a protein has more than 1 chain, they have a specific arrangement in relation to one another. ...
Protein Synthesis and Processing
Protein Synthesis and Processing

... 19. What has been removed from the pre-mRNA to make it into mRNA? introns 20. Thinking back to Model 1 and the hypothesis you developed in question 4, why do you think these regions have been removed? Because they are non-coding regions so they don’t need to be read. 21. What three bases makes up t ...
Amino acid a
Amino acid a

... 3. The Classification of 20 standard Amino Acids (very important!!!) • The name and abbreviation of amino acids – All the AAs were given a trivial (common) name. • Glutamate from wheat gluten. • Tyrosine from cheese (“tyros” in Greek). – Each AA is given a 3 letter abbreviation and 1 ...
My report on "Report Title" - RI
My report on "Report Title" - RI

... 3. How can differing electronegativities cause differences in charge across the regions of a protein’s surface? Electronegativity can be defined as an atom’s ability to attract another atom’s electrons. If electrons are not evenly shared across a protein’s surface, parts of the protein will be parti ...
Chapter 12 Pathways to biomolecules
Chapter 12 Pathways to biomolecules

... lactase – which breaks down the sugar lactose in the small intestine salivary amylase – which breaks down polysaccharides in the mouth. Almost all the chemical reactions occurring in living creatures are controlled by enzymes. Enzymes speed up the reactions that are essential for life processes by a ...
Towards the Discovery of New Antimicrobials: the Bifunctional
Towards the Discovery of New Antimicrobials: the Bifunctional

... The soluble constructs of PBP1a from Pseudomonas aeruginosa and Acinetobacter baumannii have shown to be ac@ve in both the GTase and TPase assays. Next, the full-length versions of PBP1a will be inves@gated, and whether or not the presence of the transmembrane helix affects the ac ...
Proteins
Proteins

... • Is a phosphoprotein, which has phosphate groups attached to some of the amino acid side chains. • casein is a mixture of at least three similar proteins, which differ primarily in molecular weight and amount of phosphorus they contain (number of phosphate groups). • Casein exists in milk as the ca ...
Sample Lecture Syllabus for CHEM222
Sample Lecture Syllabus for CHEM222

... a wide range of biochemical phenomena by revisiting many concepts that were covered in other chemistry and biology courses. The emphasis will be in demonstrating how these two disciplines can be integrated into a single interdisciplinary approach, to better understand and explain the world we live i ...
Amino acid analysis
Amino acid analysis

...  Proteins and peptides are macromolecules consisting of covalently bonded amino acid residues organized as a linear polymer. The sequence of the amino acids in a protein or peptide determines the properties of the molecule. ...
Document
Document

... The gap is getting bigger ...
Anti-c-myc antibody 9E10 - Protein Engineering, Design and Selection
Anti-c-myc antibody 9E10 - Protein Engineering, Design and Selection

... Fig. 2. Western blot of purified scFv 1F9 variants with myc-tag fusions. Shortened (snmyc) and shortened and mutated (mutmyc) myc-tags are compared to sc-Fv containing the original myc-tag sequence (EQKLISEEDLN). The scFv variants with the changed myc-tags have as short a tag as possible, the last t ...
Protein and Minerals in the Athlete`s Diet
Protein and Minerals in the Athlete`s Diet

... required before protein synthesis is stimulated after protein ingestion (Journal of Clinical Investigation, 1987; 80:1784-1793; Diabetes, 1996; 45:393-399; Journal of Clinical Investigation, 1987; 79:1062-1069). A slow digesting protein, such as micellar casein, may not digest fast enough to result ...


... b) protonated imidazole has twice the number of protons. c) unprotonated imidazole is invisible in the spectrum. d) the chemical shift of His differs from His+. 10. The membrane proteins that catalyze active transport reactions differ from soluble enzymes in that a) they do not enhance the rates of ...
The PYRIN domain: a novel motif found in apoptosis and
The PYRIN domain: a novel motif found in apoptosis and

... apoptosis signaling pathways, three major families of protein modules have been identified thus far: the death domain, the death effector domain (DED) and the caspase recruitment domain (CARD).2 These protein modules of approximately 100 amino acids in length function to mediate homotypic, protein-p ...
Mass Spectrometry-Based Analysis Of Membrane Proteins Derived
Mass Spectrometry-Based Analysis Of Membrane Proteins Derived

... Tan S., Tan H. T., Chung M. C. M. (2008): Membrane proteins and membrane proteomics. Proteomics, vol. 8, no. 19, 3924–3932 [Sprenger R. R., Jensen O. N. (2010): Proteomics and the dynamic plasma membrane: Quo Vadis?. Proteomics, vol. 10, no. 22, 3997–4011 Eichhorst B., Hallek M., Dreyling M. (2010): ...
Signal Transduction Pathways • Signal Transduction
Signal Transduction Pathways • Signal Transduction

2O2 - + 2H+ ------> H2O2 + O2 M3+ + O2 - ------> M2+ + O2 i
2O2 - + 2H+ ------> H2O2 + O2 M3+ + O2 - ------> M2+ + O2 i

... metal must be in the Mn III state (see reactin i above) and in this state the protein is a bright pink. The tertiary structure (right figure) is one of alpha plus beta, mostly alpha helix (red) but with three beta strands making a beta sheet (yellow). The metal (purple sphere) is held in position by ...
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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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