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some molecular basics
some molecular basics

... • Improve the functionality of the cell = selective advantage • Destroy the functionality of the cell = cell dies • Does not change the functionality of the cell = selectively ...
Molecular Interactions of Collagen-binding Proteins
Molecular Interactions of Collagen-binding Proteins

... The connective tissue is composed of cells and an extracellular matrix consisting of structural fibers and specialized proteins. The most abundant structural fiber is collagen. A collagen-fiber is comprised of bundles of collagen-fibrils, which again are comprised of individual collagen-molecules th ...
Culinary Chemistry: A Campus Cuisine Cookoff Michele McMullen R.D. Dr. Matt Queen
Culinary Chemistry: A Campus Cuisine Cookoff Michele McMullen R.D. Dr. Matt Queen

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Techniques in Protein Biochemistry

... Lecture 5: 8/29 CHAPTER 5 ...
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Four Types of Organic Molecules

... Where fats have a third fatty acid linked to glycerol, phospholipids have a negatively charged phosphate group. This makes the “head” of the phospholipid hydrophilic; the hydrocarbon “tails” are hydrophobic. Phospholipids are the major components of cell membranes. In a cell membrane, the hydrophobi ...
Macromolecules - Nolte Science
Macromolecules - Nolte Science

... specific structure and shape-conformation.  Primary structure-chain of amino acids.  Secondarycoiled/folded chain held by bonds.  Tertiary-the 3D globular shape held by bonds.  Quaternary-subunits held together. ...
Ligand Binding - Stroud -Lecture 1
Ligand Binding - Stroud -Lecture 1

... • Thermodynamics of Protein Assembly • Structural Change on complexation • Empirical fitting of Atomic Interactions with Free Energy of Association • Estimate of free energy of H bonds and charge interactions in protein complexes and role of hydrophobic effect _______________________________________ ...
condensation reaction
condensation reaction

... • LIPIDS which have four fused carbon rings with various functional groups • CHOLESTEROL IS AN IMPORTANT STERIOD – Is the precursor to many other steroids including vertebrate sex hormones and bile acids – Is the common component of animal cell membranes ...
2.3 Carbon Compounds
2.3 Carbon Compounds

... A small unit that joins with other small units to form polymers Nucleic Acid ...
(Affinity and SRM) assays for detection of potential biomarkers for
(Affinity and SRM) assays for detection of potential biomarkers for

... would next be confirmed using labelled heavy peptides. We aim to apply the developed assays to clinical samples from breast cancer patients collected at primary diagnosis and at later recurrence. If successful, it has potential to speed-up the diagnosis process for breast cancer relapse. ...
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Ch. 5 Biochemistry

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The linear sequence of amino acids (primary structure) is able to coil

... The linear sequence of amino acids (primary structure) is able to coil and fold upon itself, resulting in 3D formations such as α-helices and β-sheets. These are held together by hydrogen bonding between amino acids. The term for these 3D formations is the secondary structure of the protein. ...
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6th Grade Organic Compounds

... Name some examples of each. Compare the structures of carbohydrates, lipids, proteins, ATP and nucleic acids and relate their importance to living things ...
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Importance of Protein sorting Cell organization depend on sorting

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Chemistry of Living Things
Chemistry of Living Things

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... females make all three, just in different amounts. Steroids pass into a cell's nucleus, bind to specific receptors and genes and trigger the cell to make proteins. • Insulin, growth hormone, prolactin and other water-soluble protein hormones consist of long chains of amino acids, from several to 200 ...
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Apresentação do PowerPoint

... location at which they have no net charge. (B) The proteins form bands that can be excised and used for further experimentation. ...
x - Center for Eukaryotic Structural Genomics
x - Center for Eukaryotic Structural Genomics

... NMR structure determinations [1-4]. In the first stage, cloned DNA molecules coding for proteins of interest are transcribed and translated on a small scale (25 microL) to determine levels of protein expression and solubility. The amount of protein produced (typically 2-10 micrograms) is sufficient ...
Biochemistry
Biochemistry

... are the building blocks (monomers) of proteins.  Identify the elements that make up your amino acid. Record in your chart.  Compare your amino acid to the person next to you. Are they identical? What parts are the same? Highlight the similarities.  What part of your amino acids are different? Cir ...
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In gram negative bacteria, Outer membrane proteins synthesized in

... various OMPs into the membrane. To gain a better insight into the mechanism, by which Skp binds its client proteins in the periplasm, we designed, expressed and isolated a new Skp construct, Sx3kp, from E. coli. In this construct, the three Skp monomers were linked together with two short and flexib ...
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... • Simple proteins contain only amino acid residues. • Conjugated proteins contain amino acid residues and other organic or inorganic components (prosthetic groups). ...
Proteins, lipids, carbohydrates and nucleic acids
Proteins, lipids, carbohydrates and nucleic acids

... –  The side groups give amino acids different chemical properties. ...
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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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