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Chapter 1 Study Questions
Chapter 1 Study Questions

... 1. How are the purine bases chemically different from pyrimidine bases? 2. Distinguish between the following terms: base, nucleoside, nucleotide, and give an example of each. You may use chemical structures to illustrate your answer. 3. Compare the chemical structures of a basic amino acid (such as ...
Prescott`s Microbiology, 9th Edition Chapter 18 – Microbial
Prescott`s Microbiology, 9th Edition Chapter 18 – Microbial

... Figure 18.6 Which step (or steps) in this process is (are) replaced by PCR amplification and immobilization of fragments to a solid support in the post-Sanger sequencing techniques? Comparing this figure to 18.4, the major difference is that the Sanger steps of gel electrophoresis and cloning are re ...
23. ______ layers of ______ make up the cell
23. ______ layers of ______ make up the cell

... Proteins are made of subunits called amino acids and are used to build cells and do much of the work inside organisms. They also act as enzymes helping to control metabolic reactions in organisms. Amino acids contain two functional groups, the carboxyl group (-COOH) and the amino group (-NH2). Enzym ...
biomolecule ppt
biomolecule ppt

... • They consist of a carboxyl group (COOH) and an amino group NH2 • Peptide bonds form between amino acids (polypeptide = many peptide bonds = protein!) ...
2770 December 2007 Final Exam
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Chapter 2 Summary
Chapter 2 Summary

... and 3 are pyrimidines - cytosine, thymine, and uracil. 14. Guanine always pairs with cytosine, and Adenine always pairs with either thymine or uracil. There is always one purine and one pyrimidine in each pair. 15. Thymine is always found in DNA and uracil in RNA. 16. DNA is usually double stranded ...
Vocabulary Review
Vocabulary Review

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Amino Acids
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CENTRAL DOGMA AND GENE REGULATION
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... a. mRNA binds to the small ribosome and the first tRNA binds to the start (AUG) codon on the mRNA b. the large subunit now attaches to the small subunit c. the polypeptide chain elongates. The second tRNA molecule binds to an mRNA codon at the A site. This tRNA brings another amino acid . The riboso ...
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... Renate B. Pilz and Gerry R. Boss. University of California, San Dieqo, Department of Medicine, San Oiego, California. USA. ihen cultured human lymphoblasts are starved for an essential amino acid for 3 h, rates of purine nucleotide synthesis decrease markedly because of a decrease in the intracellul ...
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A little less conjugation, a little more accuracy
A little less conjugation, a little more accuracy

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... 25. You are interested in determining the effect of molecule X on the kinetics of an enzyme reaction. You first determined the rate at which the enzyme catalyzes a reaction by measuring the amount of product formed in a series of incubation mixtures that contained the same amount of enzyme but an in ...
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Chapter 2 - SCHOOLinSITES

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Protein Unit Study Guide/Review Sheets
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... If you have questions, make sure to ask them. Stop in before or after school. Review questions: 1. What elements comprise proteins? C, H, O, N 2. Are proteins organic? YES – CONTAIN CARBON AND HYDROGEN, THE REQUIREMENT FOR BEING AN ORGANIC MOLECULE 3. What element MAY be present in proteins? SULFUR ...
Amino acid sequence of phospholipase A from porcine pancreas
Amino acid sequence of phospholipase A from porcine pancreas

... from an inactive precursor (prophospholipase A) by the tryptic cleavage of the 7th bond (Arg-Ala) in the chain 1. Mass spectrometry showed the released heptapeptide to have the following formulaS: Pyroglu-Glu-Gly-Ile-Ser-Ser-Arg, which deviates from the originally proposed structure 1 by the reverse ...
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... Carbamoyl phosphate subsequently reacts with ornithine to form citrulline. This reaction, which catalyzed by ornithine transcarbamoylase, is driven to completion because of the release of phosphate from carbamoyl phosphate. ...
Amino acid
Amino acid

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... they are brought into the ribosome bound to tRNA molecules tRNA molecule consists of a single strand of RNA - about 80 RNA nucleotides ...
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... All of the mutants had decreased creatine kinase activity as compared to the wild-type enzyme. What information does this result provide about the reaction mechanism in the wild-type enzyme? The activity of the mutant enzyme C278D was 12-fold greater than the activity of the C278N mutant. Suggest an ...
PowerPoint Rubric: Biochemistry worksheet
PowerPoint Rubric: Biochemistry worksheet

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SP7+ P7 (1+3) Energetics and kinetics of chemical reaction.

... application of e-learning COURSE DESCRIPTION Course enrolment Passed exams from the first year of the Program. requirements and entry competences required for the course 1. Describe and explain the basic chemical bonds between the compounds and analyze and calculate the basic physicochemical princip ...
Biochemistry
Biochemistry

... Explain the difference between elements and compounds Describe the location and charge of the 3 subatomic particles (protons, neutrons and electrons) Describe what isotopes are and how radioactive isotopes are used in biology Describe the difference between a covalent and an ionic bond and explain w ...
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Transcription, Translation, and Protein Study Guide What is the

... acids fit into which group for this test.) What are the characteristics of each of these categories? How do they play a role in the formation of a protein? Hydrophobic: will turn the side chain away from water in the middle of the tertiary structure. Hydrophilic: will turn the side chain toward the ...
Amino acids and protein (lec. 2%2c 2015)
Amino acids and protein (lec. 2%2c 2015)

... named D or L according to arrangement of the groups COOH, R, NH2 and H. around the chiral α carbon atom. Sighting with the hydrogen atom away from the viewer, if these groups are arranged clockwise around the carbon atom, then it is the Dform. If counter-clockwise, it is the L-form. ...
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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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