could be made in the laboratory from inorganic substances. He used the inorganic compound ammonium cyanate. • Two major breakthroughs in the history of biochemistry are especially notable: o Roles of enzymes as catalysts o Roles of nucleic acids as information carrying molecules. 1.2 The Chemical Elements of Life • • • • • • • Six non-metallic elements: oxygen‚ carbon‚ hydrogen‚ nitrogen‚ phosphorus‚ and sulfur (CHONPS) account for more than 97% of the weight of most organisms
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b What general name is given to solutions that have many more hydrogen ions than hydroxide ions? Solutions that have many more hydrogen ions than hydroxide ions are termed acidic. 4 Name the monomers of carbohydrates‚ proteins‚ lipids and nucleic acids. The monomers (basic building blocks) of
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SBI4U – CHAPTER ONE TEST – PART A – Multiple Choice 1. Which of the following is the essential characteristic of a polar molecule? a) contains double or triple bonds b) is formed at extremely low temperatures c) contains ions as part of the structure d) has an asymmetrical distribution of electrical charge e) contains the element oxygen 2. Isomers are molecules that a) react readily with one another b) have the same molecular formula c) have different molecular masses d) differ
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proteins‚ nucleic acids‚ lipids and carbohydrates. These are mainly composed of polymers‚ long molecules made up of a large number of small‚ similar molecules‚ or monomers. Proteins are polymers of amino acids. Long amino acid chains are folded into complex shapes‚ the shape of each determining the function of the protein. They are complex organic compounds‚ essential to the functioning as well as the structure of all organic cells. Proteins range in size from a few amino acids to thousands‚ having
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LECTURE NOTES 1: Foundations of Biochemistry - 1 open ended and 5 MC Properties of living organisms - self-replication & self-assembly - sensing and resonding to changes in environment - define function for each component and regulation - Classification of organisms based on where they get their energy Phototrophs (take energy from sun light) Chemotrophs (take energy from food in environment) - organotrophs (bacteria) - not photosynthetic Biological 1) Cellular a. nucleus (eukaryotes)
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Human vs. Other Organisms # of differences in the amino acid sequence Rhesus monkey None. Horse 3: Valine‚ Glutamine‚ Alanine Donkey 3: Valine‚ Glutamine‚ Alanine Common zebra 3: Valine‚ Glutamine‚ Alanine Pig‚ cow‚ sheep 3: Valine‚ Glutamine‚ Alanine Dog 3: Valine‚ Glutamine‚ Alanine Gray whale 3: Valine‚ Glutamine‚ Alanine Rabbit 3: Valine‚ Glutamine‚ Alanine Kangaroo 3: Valine‚ Glutamine‚ Alanine Chicken‚ turkey 3: Isoleucine‚ Valine‚ Glutamine Penguin 4: Isoleucine‚ Valine‚ Glutamine
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Disease)‚ and Its Effect on the Breakdown of Amino Acids in the Human Body David Holkesvik INTRODUCTION: Branched-chain ketoaciduria‚ more commonly known as Maple syrup urine disease (MSUD) is a metabolic disorder that causes toxic buildup of un-broken down branched-chain amino acids or ketoacids. Passed on autosomal recessively‚ mutations in specific genes hinder or stop the enzyme complex responsible for normal breakdown of three amino acids found in protein-rich foods from working. The
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B. resembles the active site of general acid-base enzymes. C. resembles the transition-state structure of the normal enzyme-substrate complex. D. stabilizes the ground state for the normal enzyme-substrate complex. E. typically reacts more slowly with an enzyme than the normal substrate. 6. Which amino acid is modified in the conversion of prothrombin to thrombin? A. Glycine B. Alanine C. Arginine D. Aspartic acid E. Glutamic acid 7. Which of the following statements about
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carbohydrates‚ lipids and nucleic acid. I will also describe the functions and why they are important in our bodies. Proteins Proteins are polymers of amino acids that are joined head-to-tail in a long chain that is then folded into a three-dimensional structure unique to each type of protein. The covalent linkage between two adjacent amino acids in a protein (or polypeptide) chain is called a peptide bond. There are twenty amino acids that make up proteins. Each amino acid has a typical generic structure
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is referred to as oxyhemoglobin. Oxyhemoglobin is an unstable protein that easily reverses its’ oxygen attachments. When a molecule of hemoglobin is empty of oxygen attachments‚ it is called deoxyhemoglobin. Portions of the terminal end of the amino acids in the deoxyhemoglobin will work together to form ionic pairs. Tuesday‚ March 12‚ 13 These ionic pairs decrease the acidity of the blood by binding one hydrogen atom for every 2 oxygen molecules released. The resulting lowering of blood pH will
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