If he had more time, what would he do?

He would learn to play the guitar.

He will learn to play the guitar.

If we had a pet dinosaur, what would we name it?

This is a hypothetical situation.

If I were you, I would study harder. What does this sentence imply?

It suggests a hypothetical situation.

If we had our own spaceship, where would we explore?

We would explore distant planets.

We will explore distant planets.

We have explored distant planets.

If clause type 2 | Quizalize

If clause type 1,2,3

If-clauses type 1 and type 2

Q.1. Which of the adaptive change is characterized by the presence of One type epithelial change into another type epithelium? Atrophy Hypertrophy Metaplasia Hyperplasia Q.2. If the myocardium is deprived of oxygen supply for 10 minutes, it will develop what type of morphological change? A. Hypertrophy B. Reversible cell injury C. Irreversible cell injury D. Hyperplasia Q.3. If in a cell, nucleus shows Pyknosis, Karyolysis, which of the followings Would apply correctly? Adaptation Reversible cell injury Irreversible cell injury Q.4 Which of the following organ has greater glycolytic capacity ? A. Spleen B. Heart (Myocardium ) C. Liver D. Brain Q.5. Free radicals are produced by all of the followings EXCEPT: A. Nitric oxide, produced by endothelial cells, macrophages B. Radiant energy C. Exogenous chemicals D. Lymphocytes Q.6. The most common cause of Hemochromatosis is: A. Excessive intake of iron B. Excessive use of blood transfusions C. Excessive Hemolysis of Red blood cells Q.7. Out of the followings, one is not characteristic of Acute inflammation: A. Vasodilation B. Fibrosis C. Permeability change D. Emigration of Leukocytes Q.8. Gap between endothelial cells is facilitated by following factors EXCEPT: A. Histamine B. Leukotriens C. Nitric oxide D. Substance P Q.9. For transmigration of leukocytes, which of the following molecules plays the part? A. P-Selectin B. Integrin C. L-Selectin D. VCAM Q.10. Which are the two considered as Opsonins ? A. IgM and C5a B. IgG and C3 C. IgA and C9 D. IgE and C4

PASSIVE TRANSPORT Cell membranes help organisms maintain homeostasis by controlling what substances may enter or leave cells. Some substances can cross the cell membrane without any input of energy by the cell in a process known as passive transport. DIFFUSION The simplest type of passive transport is diffusion. Diffusion is the movement of molecules from an area of higher concentration to an area of lower concentration. This difference in the concentration of molecules across a distance is called a concentration gradient. Consider what happens when you add a sugar cube to a beaker of water. As shown in Figure 5-1, the sugar cube sinks to the bottom of the beaker. This sinking makes the concentration of sugar mole- cules greater at the bottom of the beaker than at the top. As the cube dissolves, the sugar molecules begin to diffuse slowly through the water, moving towards the lower concentration at the top. Diffusion is driven entirely by the molecules’ kinetic energy. Molecules are in constant motion because they have kinetic energy. Molecules move randomly, traveling in a straight line until they hit an object, such as another molecule. When they hit some- thing, they bounce off and move in a new direction, traveling in another straight line. If no object blocks their movement, they con- tinue on their path. Thus, molecules tend to move from areas where they are more concentrated to areas where they are less concentrated, or “down” their concentration gradient. In the absence of other influences, diffusion will eventually cause the molecules to be in equilibrium—the concentration of molecules will be the same throughout the space the molecules occupy. Returning to the example in Figure 5-1, if the beaker of water is left undisturbed, at some point the concentration of sugar molecules will be the same throughout the beaker. The sugar concentration will then be at equilibrium. SECTION 1 OBJECTIVES ● Explain how an equilibrium is established as a result of diffusion. ● Distinguish between diffusion and osmosis. ● Explain how substances cross the cell membrane through facilitated diffusion. ● Explain how ion channels assist the diffusion of ions across the cell membrane. VOCABULARY passive transport diffusion concentration gradient equilibrium osmosis hypotonic hypertonic isotonic contractile vacuole turgor pressure plasmolysis cytolysis facilitated diffusion carrier protein ion channel Sugar Water 1 2 3 FIGURE 5-1 Sugar molecules, initially in a high concentration at the bottom of a beaker, , will move about randomly through diffusion, , and eventually reach equilibrium, . At equilibrium the sugar concentration will be the same throughout the beaker. Diffusion occurs naturally because of the kinetic energy the molecules possess. 3 2 1 Copyright © by Holt, Rinehart and Winston. All rights reserved. 98 CHAPTER 5 It is important to understand that even at equilibrium the ran- dom movement of molecules continues. But because there is an equal concentration of molecules everywhere, molecules are just as likely to move in one direction as in any other. The random movements of many molecules in many directions balance one another, and equilibrium is maintained. Diffusion Across Membranes Cell membranes allow some molecules to pass through, but not others. If a molecule can pass through a cell membrane, it will diffuse from an area of higher concentration on one side of the membrane to an area of lower concentration on the other side. Diffusion across a membrane is also called simple diffusion, and only allows certain molecules to pass through the membrane. The simple diffusion of a molecule across a cell membrane depends on the size and type of molecule and on the chemical nature of the membrane. A membrane can be made, in part, of a phospho- lipid bilayer, and certain proteins can form pores in the membrane. Molecules that can dissolve in lipids may pass directly through the membrane by diffusion. For example, because of their nonpolar nature, both carbon dioxide and oxygen dissolve in lipids. Molecules that are very small but not soluble in lipids may diffuse across the membrane by moving through the pores in the membrane.

CARBOHYDRATES Carbohydrates are organic compounds composed of carbon, hydrogen, and oxygen in a ratio of about one carbon atom to two hydrogen atoms to one oxygen atom. The number of carbon atoms in a carbohydrate varies. Some carbohydrates serve as a source of energy. Other carbohydrates are used as structural materials. Carbohydrates can exist as monosaccharides, disaccharides, or polysaccharides. Monosaccharides A monomer of a carbohydrate is called a monosaccharide (MAHN-oh-SAK-uh-RIED). A monosaccharide—or simple sugar— contains carbon, hydrogen, and oxygen in a ratio of 1:2:1. The gen- eral formula for a monosaccharide is written as (CH2O)n, where n is any whole number from 3 to 8. For example, a six-carbon mono- saccharide, (CH2O)6, would have the formula C6H12O6. The most common monosaccharides are glucose, fructose, and galactose, as shown in Figure 3-6. Glucose is a main source of energy for cells. Fructose is found in fruits and is the sweetest of the monosaccharides. Galactose is found in milk. Notice in Figure 3-6 that glucose, fructose, and galactose have the same molecular formula, C6H12O6, but differing structures. The different structures determine the slightly different properties of the three compounds. Compounds like these sugars, with a single chemical formula but different structural forms, are called isomers (IE-soh-muhrz). SECTION 2 OBJECTIVES ● Distinguish between monosaccharides, disaccharides, and polysaccharides. ● Explain the relationship between amino acids and protein structure. ● Describe the induced fit model of enzyme action. ● Compare the structure and function of each of the different types of lipids. ● Compare the nucleic acids DNA and RNA. VOCABULARY carbohydrate monosaccharide disaccharide polysaccharide protein amino acid peptide bond polypeptide enzyme substrate active site lipid fatty acid phospholipid wax steroid nucleic acid deoxyribonucleic acid (DNA) ribonucleic acid (RNA) nucleotide C HO H C H OH C OH H C CH2OH H C H OH O Glucose C OH C O H OH C OH H CH2OH C H CH2OH Fructose C H HO C OH H C OH H C CH2OH H C H OH O Galactose Glucose, fructose, and galactose have the same chemical formula, but their structural differences result in different properties among the three compounds. FIGURE 3-6 Copyright © by Holt, Rinehart and Winston. All rights reserved. 56 CHAPTER 3 Disaccharides and Polysaccharides In living things, two monosaccharides can combine in a condensa- tion reaction to form a double sugar, or disaccharide (die-SAK-e-RIED). For example in Figure 3-4, the monosaccharides fructose and glu- cose can combine to form the disaccharide sucrose. A polysaccharide is a complex molecule composed of three or more monosaccharides. Animals store glucose in the form of the polysaccharide glycogen. Glycogen consists of hundreds of glucose molecules strung together in a highly branched chain. Much of the glucose that comes from food is ultimately stored in your liver and muscles as glycogen and is ready to be used for quick energy. Plants store glucose molecules in the form of the polysaccha- ride starch. Starch molecules have two basic forms—highly branched chains that are similar to glycogen and long, coiled, unbranched chains. Plants also make a large polysaccharide called cellulose. Cellulose, which gives strength and rigidity to plant cells, makes up about 50 percent of wood. In a single cellu- lose molecule, thousands of glucose monomers are linked in long, straight chains. These chains tend to form hydrogen bonds with each other. The resulting structure is strong and can be broken down by hydrolysis only under certain conditions. PROTEINS Proteins are organic compounds composed mainly of carbon, hydrogen, oxygen, and nitrogen. Like most of the other biological macromolecules, proteins are formed from the linkage of monomers called amino acids. Hair and horns, as shown in Figure 3-7a, are made mostly of proteins, as are skin, muscles and many biological catalysts (enzymes). Amino Acids There are 20 different amino acids, and all share a basic structure. As Figure 3-7b shows, each amino acid contains a central carbon atom covalently bonded to four other atoms or functional groups. A single hydrogen atom, highlighted in blue in the illustration, bonds at one site. A carboxyl group, —COOH, highlighted in green, bonds at a second site. An amino group, —NH2, highlighted in yel- low, bonds at a third site. A side chain called the R group, high- lighted in red, bonds at the fourth site. The main difference among the different amino acids is in their R groups. The R group can be complex or it can be simple, such as the CH3 group shown in the amino acid alanine in Figure 3-7b. The differences among the amino acid R groups gives different proteins very different shapes. The different shapes allow pro- teins to carry out many different activities in living things. Amino acids are commonly shown in a simplified way such as balls, as shown in Figure 3-7c. (a) Many structures, such as hair and horns are made of proteins. (b) Proteins are made up of amino acids. Amino acids differ only in the type of R group (shown in red) they carry. Polar R groups can dissolve in water, but nonpolar R groups cannot. (c) Amino acids have complex structures, so, in this and other textbooks, they are often simplified into balls. FIGURE 3-7 (b) Alanine (an amino acid) (c) Simplified version of amino acid CH3 H N OH C C H O H (a) Copyright © by Holt, Rinehart and Winston. All rights reserved. BIOCHEMISTRY 57 H H N C C OH H O H CH3 H2O Glycine Alanine H N OH C C H O H H H N C C H O H CH3 N OH C C H O H (a) (b) (a) The peptide bond (shaded blue) that binds amino acids together to form a polypeptide results from a condensation reaction that produces water. (b) Poly- peptides are commonly shown as a string of balls in this textbook and elsewhere. Each ball represents an amino acid. FIGURE 3-8 Substrate Products Enzyme 1 2 3 In the induced fit model of enzyme action, the enzyme can attach only to a substrate (reactant) with a specific shape. The enzyme then changes and reduces the activation energy of the reaction so reactants can become products. The enzyme is unchanged and is available to be used again. 3 2 1 FIGURE 3-9 Dipeptides and Polypeptides Figure 3-8a shows how two amino acids bond to form a dipeptide (die-PEP-TIED). In this condensation reaction, the two amino acids form a covalent bond, called a peptide bond (shaded in blue in Figure 3-8a) and release a water molecule. Amino acids often form very long chains called polypeptides (PAHL-i-PEP-TIEDZ). Proteins are composed of one or more polypep- tides. Some proteins are very large molecules, containing hun- dreds of amino acids. Often, these long proteins are bent and folded upon themselves as a result of interactions—such as hydrogen bonding—between individual amino acids. Protein shape can also be influenced by conditions such as temperature and the type of solvent in which a protein is dissolved. For exam- ple, cooking an egg changes the shape of proteins in the egg white. The firm, opaque result is very different from the initial clear, runny material. Enzymes Enzymes—RNA or protein molecules that act as biological catalysts—are essential for the functioning of any cell. Many enzymes are proteins. Figure 3-9 shows an induced fit model of enzyme action. Enzyme reactions depend on a physical fit between the enzyme molecule and its specific substrate, the reactant being catalyzed. Notice that the enzyme has folds, or an active site, with a shape that allows the substrate to fit into the active site. An enzyme acts only on a specific substrate because only that substrate fits into its active site. The linkage of the enzyme and substrate causes a slight change in the enzyme’s shape. The change in the enzyme’s shape weakens some chemical bonds in the substrate, which is one way that enzymes reduce activation energy, the energy needed to start the reaction. After the reaction, the enzyme releases the products. Like any catalyst, the enzyme itself is unchanged, so it can be used many times. An enzyme may not work if its environment is changed. For example, change in temperature or pH can cause a change in the shape of the enzyme or the substrate. If such a change happens, the reaction that the enzyme would have catalyzed cannot occur.

Related quizzes

Related quizzes