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[DOWNLOAD] Chapter 3 Test Biochemistry Answers
Therefore, you should not rely on sample tests as precise guides to test content. Approximate coverage of each test is shown below. For more practice questions, see the Practice quizzes. Information about the note page , which you may use on all...
Biology Study Guide For The Chapter 3 Test On Biochemistry
Each functional group gives the molecules its own identity and purpose. They are as follows: hydroxyl, carboxyl, amino, and phosphate. Compare how organic compounds are built to how they are broken down. When macromolecules of polymers are formed, the condensation reaction is responsible for the bonding that takes place. In the situation where the polymers that make up macromolecules need to be broken down, the hydrolysis reaction breaks them apart. Explain the role of ATP in cellular activities. ATP Adenosine Triphosphate levels represent how much energy is present in the living thing. Food is chemically broken down to get the ATP energy molecules necessary for survival. List the 4 major classes of organic compounds. Functional groups are clusters of atoms that influence or determine the characteristics of the molecules they create. Describe the general structure of carbohydrates. Define the term isomer. Summarize the differences between simple sugars, double sugars, and complex sugars.
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Biochemistry
This is why amino acids create proteins. State the basic structure of an amino acid. Compare the processes used in the formation of a dipeptide and disaccharide. Summarize the induced fit model of enzyme activity. Differentiate between saturated and unsaturated triglycerides. Compare the structures of triglycerides, phosphates, lipids, and steroids. This picture below is the triglyceride This picture is a phosphate. This picture is a lipid. State how steroids differ from other lipids. Identify an important characteristic of waxes. They are also a part of enzymes vent microorganisms from entering the ear canal. Compare the two kinds of nucleic acids. Name the 3 parts of a nucleotide. Concept Mapping between: dipeptide, triglycerides, RNA, phospholipid, carbohydrates, monosaccharide, amino acid, disaccharide, polypeptide, polysaccharide, proteins, DNA, lipids, nucleic acids, steroids, and waxes.
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Campbell's Biology, 8th Edition
Omega-3 fatty acids have which of the following? A Nonenzymatic glycosylation or glycation creates glycoproteins by the chemical addition of sugars to polypeptides. Since this type of glycosylation is nonenzymatic, the time and the concentration of sugar control glycosylation. Because people with higher circulating levels of glucose have higher levels of nonenzymatic glycosylation, measurement of the glycosylated hemoglobin A1c is a diagnostic test used to monitor blood sugar levels in persons with diabetes.
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Chapter 3 Test - Chemistry
C Ribose is a pentose, a simple sugar monosaccharide that has five carbon atoms per molecule. It is synthesized in the body and obtained in small amounts from consumption of ripe fruits and vegetables. Deoxyribose, a component of DNA, also is a pentose. D The optimum pH for enzymes varies for different enzymes and even enzymes with similar actions may have different optimal pH based on where they act. For example, trypsin, a digestive enzyme that acts in the small intestine has an optimal pH of 8 while pepsin, which acts in the more acidic milieu of the stomach, has an optimal pH of 2. B A catabolic enzyme engages in destructive metabolism, which involves degrading or breaking down complex molecules into simpler ones with the resulting release of energy. In the body, the breakdown of food in the gastrointestinal tract by a variety of digestive enzymes is an example of a catabolic process.
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Isomerism Questions And Answers Pdf
The opposite of catabolism is anabolism. C Anabolism is the opposite of catabolism and is a set of metabolic pathways that serve to create, construct, or synthesize larger molecules from smaller ones, such as the synthesis of carbohydrates, proteins and fatty acids. Anabolic processes consume or require energy rather than releasing energy. Examples of anabolic processes include gluconeogenesis, glyoxylate cycle, and glycosylation. C Allosteric enzymes change their configurations when they bind with cofactors.
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CH450 And CH451: Biochemistry - Defining Life At The Molecular Level
Their catalytic activity is altered — either enhanced or reduced — by binding of specific ligands at sites other than the substrate-binding site. When catalytic activity of the enzyme is enhanced, the effector is termed an activator; when it is diminished or eliminated, it is called a deactivator or inhibitor. D Proteolytic enzymes, also known as proteases, catalyze the splitting or breakdown of proteins into smaller peptide fractions and amino acids. The process of accomplishing this breakdown is called proteolysis. Peptidases are a subgroup of proteases that that catalyze the hydrolysis of peptide linkages; they are present in plants and yeast and in the body. In the body, they are involved in digestion. B Amylase is the class of enzymes involved in the breakdown and digestion of starches — complex carbohydrates — into simple sugars to supply energy. Amylases are glycoside hydrolases and act on? Plants and some bacteria make amylases. In the body, they are present in saliva and are produced by salivary glands and the pancreas.
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Easy Biology Class
C The stable three-dimensional shape and orientation of a protein its unique folds, termed its native configuration determine its function and chemical reactivity. Proteins are composed of series of as many as twenty different L-? Proteins are distinguished by their configurations into three broad classes — globular proteins, fibrous proteins, and membrane proteins. D The biosynthesis of a protein molecule uses information encoded in genes. The amino acid sequence of the protein is delineated by the nucleotide sequence of the gene that encodes the protein.
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CHEM 2770 / MBIO 2770
Codons, sequences of three adjacent nucleotides along a DNA or messenger RNA molecule, designate the specific amino acid to be incorporated into a polypeptide. C Peptide bonds are the primary linkages of all proteins. They are the chemical connections that form between the carboxyl group COOH of one amino acid and the amino group NH2 of adjacent amino acids. A dipeptide contains two amino acids, a tripeptide three, a tetrapeptide four, and so on. The products of protein catabolism are used to synthesize new amino acids or are converted to other compounds via the citric acid cycle. Protein catabolism is most often carried out by proteases. A The citric acid cycle, also known as the tricarboxylic acid cycle TCA cycle , the Krebs cycle, or the Szent-Gyorgyi-Krebs cycle is a key component of the metabolic pathways that chemically converts proteins, carbohydrates, and fats into usable energy.
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It is called citric acid cycle because the citric acid is the first product and the final reactant of the metabolic pathway. D The substrate of the citric acid cycle is acetyl coenzyme A. It is derived from glycolysis by a decarboxylating dehydrogenase activity of pyruvate dehydrogenase. The cycle yields the following intermediates: citrate, cis-aconitate, iso-citrate, alpha-ketoglutarate, succinyl-CoA, succinate, fumarate, malate, and oxaloacetate.
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Biochemistry Practice Questions
At the conclusion of each cycle, the four-carbon oxaloacetate has been regenerated, and the cycle begins again. D Adenosine triphosphate ATP is an energy-filled nucleotide that powers the cells and stores energy. It is present in all life forms, from simple, single-celled organisms to humans. Organisms catabolize carbohydrates to create ATP. Then, the ATP is used for anabolic cellular reactions. Each molecule of glucose can be catabolized to as many as 34 molecules of ATP. B Oxidative phosphorylation is a biochemical process that takes place in cells at a plasma membrane. The final metabolic pathway of cellular respiration, it occurs after glycolysis and the citric acid cycle.
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CHE 120 - Introduction To Organic Chemistry - Textbook
As many as 26 of 30 ATP molecules generated from a single glucose molecule during cellular respiration result from the process of oxidative phosphorylation. C The reduced intermediaries of the citric acid cycle are the source for multiple biosynthetic pathways. Every round of the cycle joins an acetyl group to oxaloacetate, oxidizing two carbons off as Co2, which leaves succinate. Succinate is converted back to oxaloacetate producing one GTP and reduced cofactors. The rate of the cycle is determined by the availability of substrates, inhibition of accumulating products and allosteric inhibition of enzymes. A Free or unesterified fatty acids are released by the hydrolysis of triglycerides within adipose tissue. Free fatty acids can be used as an immediate source of energy by multiple organs and tissue and can be converted by the liver into ketone bodies.
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Online Ramadan Quiz
Because free fatty acids can interact with a variety of enzyme systems, they must be rapidly sequestered in tissues to ensure that their activities are closely regulated. C An ester is formed when an alcohol combines with an acid in a reaction to form an organic compound. While fatty acids occur in nature in their free unesterified state, they are most often found as esters linked to glycerol, cholesterol, or long-chain aliphatic alcohols and as amides in sphingolipids. C Omega-3 fatty acids have a final carbon-carbon double bond in the third bond from the methyl end of the fatty acid. Omega-3 fatty acids — eicosapentaenoic acid and docosahexaenoic acid may be derived from the diet. They are present in oily or fatty fish, such as salmon, tuna, sardines, trout, and mackerel, and alpha linolenic acid is derived from plants.
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Chapter Fluid, Electrolyte, And Acid-Base Balance
A B C D E alanine; is a simple methyl group glycine; is a hydrogen atom glycine; is unbranched lysine; contains only nitrogen proline; forms a covalent bond with the amino group 3. Amino acids Pages: Difficulty: 3 Ans: C Which of the following statements about aromatic amino acids is correct? A All are strongly hydrophilic. B Histidines ring structure results in its being categorized as aromatic or basic, depending on pH. C On a molar basis, tryptophan absorbs more ultraviolet light than tyrosine. D The major contribution to the characteristic absorption of light at nm by proteins is the phenylalanine R group. E The presence of a ring structure in its R group determines whether or not an amino acid is aromatic. Amino acids Page: 80 Difficulty: 2 Ans: A Which of the following statements about cystine is correct?
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Answer Key Chapter 3 - Microbiology | OpenStax
B Cystine is an example of a nonstandard amino acid, derived by linking two standard amino acids. C Cystine is formed by the oxidation of the carboxylic acid group on cysteine. D Cystine is formed through a peptide linkage between two cysteines. Chapter 3 Amino Acids, Peptides, and Proteins 23 9. Amino acids Page: 84 Difficulty: 3 Ans: B 1What is the approximate charge difference between glutamic acid and -ketoglutarate at pH 9. A B C D E cleavage condensation group transfer isomerization oxidation reduction Peptides and proteins Page: 86 Difficulty: 1 Ans: C An octapeptide composed of four repeating glycylalanyl units has: A one free amino group on an alanyl residue.
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CHEM1120 Test Bank Of Old Quizzes And Exams
B one free amino group on an alanyl residue and one free carboxyl group on a glycyl residue. C one free amino group on a glycyl residue and one free carboxyl group on an alanyl residue. D two free amino and two free carboxyl groups. E two free carboxyl groups, both on glycyl residues. Peptides and proteins Pages: Difficulty: 2 Ans: C Which of the following is correct with respect to the amino acid composition of proteins? A Larger proteins have a more uniform distribution of amino acids than smaller proteins. Chapter 3 Amino Acids, Peptides, and Proteins 25 B Proteins contain at least one each of the 20 different standard amino acids. C Proteins with different functions usually differ significantly in their amino acid composition. D Proteins with the same molecular weight have the same amino acid composition. E The average molecular weight of an amino acid in a protein increases with the size of the protein.
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Biochemistry ; Questions And Answers
Peptides and proteins Page: 87 Difficulty: 2 Ans: B The average molecular weight of the 20 standard amino acids is , but biochemists use when estimating the number of amino acids in a protein of known molecular weight. A The number is based on the fact that the average molecular weight of a protein is , with an average of 1, amino acids. B The number reflects the higher proportion of small amino acids in proteins, as well as the loss of water when the peptide bond forms. C The number reflects the number of amino acids found in the typical small protein, and only small proteins have their molecular weight estimated this way. D The number takes into account the relatively small size of nonstandard amino acids. E The number represents the molecular weight of conjugated amino acids.
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Chapter 3 Biochemistry Studyguide - BIOLOGY JUNCTION
Peptides and proteins Page: 88 Difficulty: 1 Ans: B Which of the following refers to particularly stable arrangements of amino acid residues in a protein that give rise to recurring patterns? Peptides and proteins Page: 88 Difficulty: 1 Ans: D Which of the following describes the overall three-dimensional folding of a polypeptide? Working with proteins Page: 91 Difficulty: 2 Ans: B In a mixture of the five proteins listed below, which should elute second in size-exclusion gelfiltration chromatography? Working with proteins Page: 93 Difficulty: 2 Ans: B To determine the isoelectric point of a protein, first establish that a gel: Chapter 3 Amino Acids, Peptides, and Proteins 27 A contains a denaturing detergent that can distribute uniform negative charges over the proteins surface.
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Chapter 3 Biochemistry Studyguide
B exhibits a stable pH gradient when ampholytes become distributed in an electric field. C is washed with an antibody specific to the protein of interest. D neutralizes all ionic groups on a protein by titrating them with strong bases. E relates the unknown protein to a series of protein markers with known molecular weights, Mr. Working with proteins Pages: Difficulty: 3 Ans: A The first step in two-dimensional gel electrophoresis generates a series of protein bands by isoelectric focusing. In a second step, a strip of this gel is turned 90 degrees, placed on another gel containing SDS, and electric current is again applied. In this second step: A proteins with similar isoelectric points become further separated according to their molecular weights. B the individual bands become stained so that the isoelectric focus pattern can be visualized. C the individual bands become visualized by interacting with protein-specific antibodies in the second gel.
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Cell Physiology Chapter 3 Test
D the individual bands undergo a second, more intense isoelectric focusing. E the proteins in the bands separate more completely because the second electric current is in the opposite polarity to the first current. Working with proteins Pages: Difficulty: 1 Ans: B The term specific activity differs from the term activity in that specific activity: A B C D E is measured only under optimal conditions. The covalent structure of proteins Page: 96 Difficulty: 1 Ans: B The functional differences, as well as differences in three-dimensional structures, between two different enzymes from E.
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Chemistry For Biologists
B amino acid sequences. C roles in DNA metabolism. D roles in the metabolism of E. E secondary structures. The covalent structure of proteins Page: 99 Difficulty: 2 Ans: C One method used to prevent disulfide bond interference with protein sequencing procedures is: A cleaving proteins with proteases that specifically recognize disulfide bonds. C reducing disulfide bridges and preventing their re-formation by further modifying the SH groups. D removing cystines from protein sequences by proteolytic cleavage. E sequencing proteins that do not contain cysteinyl residues. When the native peptide was exposed to cyanogen bromide CNBr , an octapeptide and free glycine were recovered. Incubation of the native peptide with trypsin gave a pentapeptide, a tripeptide, and free Lys. Digestion with the enzyme pepsin produced a dipeptide, a tripeptide, and a tetrapeptide.
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Campbell's Biology, 8th Edition | CourseNotes
The tetrapeptide was composed of Lys 2, Phe, and Gly. The covalent structure of proteins Page: Difficulty: 1 Ans: C Even when a gene is available and its sequence of nucleotides is known, chemical studies of the protein are still required to determine: A B C D E molecular weight of the protein. The covalent structure of proteins Chapter 3 Amino Acids, Peptides, and Proteins 29 Pages: Difficulty: 2 Ans: C A major advance in the application of mass spectrometry to macromolecules came with the development of techniques to overcome which of the following problems? A Macromolecules were insoluble in the solvents used in mass spectrometry. B Mass spectrometric analyses of macromolecules were too complex to interpret. C Mass spectrometric analysis involved molecules in the gas phase.
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Test Bank For Lehninger Principles Of Biochemistry 6e Nelson
D Most macromolecules could not be purified to the degree required for mass spectrometric analysis. E The specialized instruments required were prohibitively expensive. Protein sequences and evolution Pages: Difficulty: 3 Ans: A Compare the following sequences taken from four different proteins, and select the answer that best characterizes their relationships. B Comparing proteins 1 and 2 in column A reveals that these two proteins have diverged the most throughout evolution. C Protein 4 is the protein that shows the greatest overall homology to protein 1. D Proteins 2 and 3 show a greater evolutionary distance than proteins 1 and 4.
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Chapter 3 - Biochemistry | Biology Quiz - Quizizz
E The portions of amino acid sequence shown suggest that these proteins are completely unrelated. Short Answer Questions Amino acids Page: 76 Difficulty: 1 What are the structural characteristics common to all amino acids found in naturally occurring proteins? Ans: All amino acids found in naturally occurring proteins have an carbon to which are attached a carboxylic acid, an amine, a hydrogen, and a variable side chain.
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CHEM Practice Exams - NIU - Department Of Chemistry And Biochemistry
All the amino acids are also in the L configuration. Amino acids Page: 79 Difficulty: 1 Only one of the common amino acids has no free -amino group. Name this amino acid and draw its structure. Ans: The amino acid L-proline has no free -amino group, but rather has an imino group formed by cyclization of the R-group aliphatic chain with the amino group see Fig. Amino acids Pages: Difficulty: 2 Briefly describe the five major groupings of amino acids. Ans: Amino acids may be categorized by the chemistry of their R groups: 1 nonpolar aliphatics; 2 polar, uncharged; 3 aromatic; 4 positively charged; 5 negatively charged.
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MCAT Biochemistry: Everything You Need To Know — Shemmassian Academic Consulting
See Fig. Amino acids Page: 79 Difficulty: 2 Draw the structures of the amino acids phenylalanine and aspartate in the ionization state you would expect at pH 7. Why is aspartate very soluble in water, whereas phenylalanine is much less soluble? Ans: Aspartate has a polar hydrophilic side chain, which forms hydrogen bonds with water. In contrast, phenylalanine has a nonpolar hydrophobic side chain. Amino acids Page: 80 Difficulty: 3 Name two uncommon amino acids that occur in proteins. By what route do they get into proteins? Ans: Some examples are 4-hydroxyproline, 5-hydroxylysine, -carboxyglutamate, N-methyllysine, desmosine, and selenocysteine. Uncommon amino acids in proteins other than selenocysteine usually result from chemical modifications of standard amino acid R groups after a protein has been synthesized.
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Chapter 3 Test Biochemistry Answers
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