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Aromatic compounds of biological importance
Aromatic compounds of biological importance

... subunits with respect to one another. Interaction between subunits is mediated by noncovalent forces, such as hydrogen bonds and hydrophobic interactions. ...
circular dichroism
circular dichroism

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... Proteins are first separated across a gel according to their isoelectric point, then separated in a perpendicular direction on the basis of their molecular weight. Electrophoresis in which a second perpendicular electrophoretic transport is performed on the separate components resulting from the fir ...
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4.9.teaching.notes

ORGANELLES AND PROTEIN SYNTHESIS Worksheet #3
ORGANELLES AND PROTEIN SYNTHESIS Worksheet #3

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CHM 103 Lecture 36 S07
CHM 103 Lecture 36 S07

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Slide 1

... Acids, Bases, and Salts  Acid  A solute that adds hydrogen ions to a solution  Strong acids dissociate completely in solution ...
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HANDOUT: CH 17 pt 1 Study
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The four types of nucleotides in DNA are Adenine, Thymine

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Cheese Lab - Protein Chemistry
Cheese Lab - Protein Chemistry

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0d56a389a26e40f78a6bc73c6f2bab172a69bf20

... In a n ionic bond the atoms are bound together through an attraction between oppositely charged ions, in a covalent bond the atoms are bound together by shared electrons 2. What are the three parts of an atom, and what are the charges of each part? Protons, neutrons and electrons 3. Which atoms does ...
CHAPTER 17 FROM GENE TO PROTEIN I. Student misconceptions
CHAPTER 17 FROM GENE TO PROTEIN I. Student misconceptions

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bonds form when water is removed to hold acids together.
bonds form when water is removed to hold acids together.

... 23. Amino acids are linked together to make proteins by removing a molecule of _____________ in a process called __________________. 24. Chains of amino acids make ________________________ which can join together to make a _____________________. 25. _______________ bonds form when water is removed t ...
Biological Macromolecules
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... Primary structure is the sequence of amino acids in a polypeptide (Usually read N-C) Secondary structures are localized folds or helices that form within a region of a polypeptide Tertiary structures are larger folding events that are stabilized by interactions between R groups Quaternary structure ...
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Lipids - Cloudfront.net
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Ass4 - The University of Sydney
Ass4 - The University of Sydney

... Protein kinase C could be activated via both growth factor and 7-TMS receptor signalling Protein kinase C becomes activated after dissociation of its regulatory subunits Phospholipase C hydrolyses phospholipids in the ER membrane, leading to Ca2+ release Diacyl glycerol is phosphorylated and becomes ...
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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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