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Proteins
Proteins

... • . essential life substance of all living matter . • act as structural unit to build our bodies . • specific structural chemical units amino acids • amino [alkaline substance carbon, hydrogen ,o2& NH2. ...
This exam has 9 pages, including this one.
This exam has 9 pages, including this one.

... Part A: (14 points total: 2 points each, Circle the best answer) 1. Which of the following group can serve as an effective donor of hydrogen bonds. a) N-H b) C-H c) S-H d) C=O 2. A tri-protic weak acid can act as an effective buffer a) at all pH values. b) when the pH is approximately equal to any o ...
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paper - ap pgecet

... To immobilise an enzyme in a durable way, Diazolation is frequently used, which of the following statement is correct for Diazolation ? (A) Reaction occurs between the amino group of the support and the carboxyl group of the enzyme (B) A bifunctional or multi-functional reagent used to create bondin ...
DNA Synthesis (Replication)
DNA Synthesis (Replication)

...  The role of tRNA is to specify which sequence from the genetic code corresponds to which amino acid  One end of the tRNA complements the genetic code in a threenucleotide sequence called the anticodon  On the other end of the tRNA is a covalent attachment to the amino acid that corresponds to th ...
Lecture Slides for Fatty Acid Catabolism
Lecture Slides for Fatty Acid Catabolism

Name Date AP Biology – Metabolism and Enzymes Review When a
Name Date AP Biology – Metabolism and Enzymes Review When a

... c. the forward and the backward reactions have stopped. d. ΔG = 0 e. All of the above are true. 6. An endergonic reaction could be described as one that a. proceeds spontaneously with the addition of activation energy. b. produces products with more free energy than the reactants. c. is not able to ...
Proteins2[1]
Proteins2[1]

... chain including side chains • It includes the folding of secondary structure (α helix and β sheets) and side chains • Helices and sheets can be combined to form tertiary structure • It is the final arrangement of domains in the polypetide ...
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Proteins - Many Structures, Many Functions
Proteins - Many Structures, Many Functions

... Distinguish proteins from the other classes of macromolecules and list the biological functions which members of this class perform List and be able to recognize the four major components of a typical amino acid and explain how amino acids may be grouped according to the nature of their side chain ...
Case study - Castle High School
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... Waxes, found on the surfaces of plants and aquatic bird feathers, help prevent evaporation of water from the cells of the organism. ...
genetic code and tra..
genetic code and tra..

... the finished protein must be present at the time of protein synthesis. 2- Ribosomes: the site of protein synthesis. They are large complexes of protein and rRNA. In human, they consist of two subunits, one large (60S) and one small (40S). 3- tRNA: at least one specific type of tRNA is required to tr ...
Understanding an Enzyme Active Site
Understanding an Enzyme Active Site

... alpha helices and/or beta sheets (secondary structure) connected by short turns of less regular protein structure. In the space below, draw and label examples of primary, secondary and tertiary structures. ...
Biochemistry
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IUPAC-IUB Commission on Biochemical Nomenclature
IUPAC-IUB Commission on Biochemical Nomenclature

... proteini. A fragmentary sequence is to be preceded or followed by a slash (/) to indicate that it is not known to be the end of the complete protein (see comment in section 8.2). 3.2. Initial letters are used where there is no ambiguity. There are six such cases: cysteine, histidine, isoleucine, met ...
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Biochemistry - ScienceGeek.net

... whereas glycogen is a branched chain of glucose units. ...
Biomolecule Reading
Biomolecule Reading

... Enzymes are special proteins that help chemical reactions happen faster by decreasing the activation energy of the chemical reaction. Activation energy is the amount of energy needed before a chemical reaction can start. By lowering the activation energy of chemical reactions, enzymes help cells bui ...
Course Syllabus AG 408 – Nutritional Biochemistry Spring Semester, 2013 MWF 12:00-12:50
Course Syllabus AG 408 – Nutritional Biochemistry Spring Semester, 2013 MWF 12:00-12:50

... and the integration of metabolic systems. Included also will be the chemistry of nitrogenous bases and how transcription and translation is accomplished on the cellular level. Student Learning Outcomes: Students will learn the biochemical mechanisms of nutrition and metabolism. Student progress will ...
CH_18_8_Degradation_Amino_Acids
CH_18_8_Degradation_Amino_Acids

... Match each the intermediate with the amino acid that provides its carbon skeleton: pyruvate, fumarate, or ketoglutarate. A. B. C. D. ...
In Vitro Protein Synthesis of Perdeuterated Proteins for NMR Studies
In Vitro Protein Synthesis of Perdeuterated Proteins for NMR Studies

... E. coli cell extracts should in principle also be applicable with other cellfree systems, for example, with wheat germ or insect cell extract for the production of eukaryotic proteins. ...
facts about maple syrup urine disease (msud)
facts about maple syrup urine disease (msud)

Proteins*
Proteins*

...  Two amino acids linked together are called dipeptides  More than 2 linked together are called polypeptides polypeptides can be thousands of amino acids long ...
Chapter 5: Microbial Metabolism
Chapter 5: Microbial Metabolism

... and molecular subunits (example: amino acids from proteins) Anabolism = building of macromolecules that the organism needs (proteins from amino acid subunits or DNA from nucleotides) ...
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Amino acid synthesis

Amino acid synthesis is the set of biochemical processes (metabolic pathways) by which the various amino acids are produced from other compounds. The substrates for these processes are various compounds in the organism's diet or growth media. Not all organisms are able to synthesise all amino acids. Humans are excellent example of this, since humans can only synthesise 11 of the 20 standard amino acids (aka non-essential amino acid), and in time of accelerated growth, arginine, can be considered an essential amino acid.A fundamental problem for biological systems is to obtain nitrogen in an easily usable form. This problem is solved by certain microorganisms capable of reducing the inert N≡N molecule (nitrogen gas) to two molecules of ammonia in one of the most remarkable reactions in biochemistry. Ammonia is the source of nitrogen for all the amino acids. The carbon backbones come from the glycolytic pathway, the pentose phosphate pathway, or the citric acid cycle.In amino acid production, one encounters an important problem in biosynthesis, namely stereochemical control. Because all amino acids except glycine are chiral, biosynthetic pathways must generate the correct isomer with high fidelity. In each of the 19 pathways for the generation of chiral amino acids, the stereochemistry at the α-carbon atom is established by a transamination reaction that involves pyridoxal phosphate. Almost all the transaminases that catalyze these reactions descend from a common ancestor, illustrating once again that effective solutions to biochemical problems are retained throughout evolution.Biosynthetic pathways are often highly regulated such that building-blocks are synthesized only when supplies are low. Very often, a high concentration of the final product of a pathway inhibits the activity of enzymes that function early in the pathway. Often present are allosteric enzymes capable of sensing and responding to concentrations of regulatory species. These enzymes are similar in functional properties to aspartate transcarbamoylase and its regulators. Feedback and allosteric mechanisms ensure that all twenty amino acids are maintained in sufficient amounts for protein synthesis and other processes.
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