However, fats do have important functions. Fats serve as long-term energy storage. They also provide insulation for the body. Phospholipids are the major constituent of the plasma membrane. Like fats, they are composed of fatty acid chains attached to a glycerol or similar backbone. Instead of three fatty acids attached, however, there are two fatty acids and the third carbon of the glycerol backbone is bound to a phosphate group. The phosphate group is modified by the addition of an alcohol.
A phospholipid has both hydrophobic and hydrophilic regions. The fatty acid chains are hydrophobic and exclude themselves from water, whereas the phosphate is hydrophilic and interacts with water. Cells are surrounded by a membrane, which has a bilayer of phospholipids. The fatty acids of phospholipids face inside, away from water, whereas the phosphate group can face either the outside environment or the inside of the cell, which are both aqueous. Because fat is the most calorie dense food and having a storable, high calorie compact energy source would be important to survival.
The nature of its fat also made it an important trade good. Like salmon, ooligan returns to its birth stream after years at sea. Its arrival in the early spring made it the first fresh food of the year. As you learned above all fats are hydrophobic water hating. To isolate the fat, the fish is boiled and the floating fat skimmed off.
Importantly it is a solid grease at room temperature. Because it is low in polyunsaturated fats which oxidize and spoil quickly it can be stored for later use and used as a trade item. Its composition is said to make it as healthy as olive oil, or better as it has omega 3 fatty acids that reduce risk for diabetes and stroke. It also is rich in three fat soluble vitamins A, E and K. Unlike the phospholipids and fats discussed earlier, steroids have a ring structure.
Although they do not resemble other lipids, they are grouped with them because they are also hydrophobic. All steroids have four, linked carbon rings and several of them, like cholesterol, have a short tail. Cholesterol is a steroid. Cholesterol is mainly synthesized in the liver and is the precursor of many steroid hormones, such as testosterone and estradiol. It is also the precursor of vitamins E and K.
Cholesterol is the precursor of bile salts, which help in the breakdown of fats and their subsequent absorption by cells. Although cholesterol is often spoken of in negative terms, it is necessary for the proper functioning of the body. It is a key component of the plasma membranes of animal cells. Waxes are made up of a hydrocarbon chain with an alcohol —OH group and a fatty acid. Examples of animal waxes include beeswax and lanolin.
Plants also have waxes, such as the coating on their leaves, that helps prevent them from drying out. Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules.
Proteins may be structural, regulatory, contractile, or protective; they may serve in transport, storage, or membranes; or they may be toxins or enzymes.
Each cell in a living system may contain thousands of different proteins, each with a unique function. Their structures, like their functions, vary greatly. They are all, however, polymers of amino acids, arranged in a linear sequence.
The functions of proteins are very diverse because there are 20 different chemically distinct amino acids that form long chains, and the amino acids can be in any order. For example, proteins can function as enzymes or hormones. Enzymes , which are produced by living cells, are catalysts in biochemical reactions like digestion and are usually proteins. Each enzyme is specific for the substrate a reactant that binds to an enzyme upon which it acts.
Enzymes can function to break molecular bonds, to rearrange bonds, or to form new bonds. An example of an enzyme is salivary amylase, which breaks down amylose, a component of starch.
Hormones are chemical signaling molecules, usually proteins or steroids, secreted by an endocrine gland or group of endocrine cells that act to control or regulate specific physiological processes, including growth, development, metabolism, and reproduction. For example, insulin is a protein hormone that maintains blood glucose levels.
Proteins have different shapes and molecular weights; some proteins are globular in shape whereas others are fibrous in nature. For example, hemoglobin is a globular protein, but collagen, found in our skin, is a fibrous protein. Protein shape is critical to its function. Changes in temperature, pH, and exposure to chemicals may lead to permanent changes in the shape of the protein, leading to a loss of function or denaturation to be discussed in more detail later.
All proteins are made up of different arrangements of the same 20 kinds of amino acids. Amino acids are the monomers that make up proteins. Each amino acid has the same fundamental structure, which consists of a central carbon atom bonded to an amino group —NH 2 , a carboxyl group —COOH , and a hydrogen atom. Every amino acid also has another variable atom or group of atoms bonded to the central carbon atom known as the R group.
The R group is the only difference in structure between the 20 amino acids; otherwise, the amino acids are identical. The chemical nature of the R group determines the chemical nature of the amino acid within its protein that is, whether it is acidic, basic, polar, or nonpolar. Each amino acid is attached to another amino acid by a covalent bond, known as a peptide bond, which is formed by a dehydration reaction. The carboxyl group of one amino acid and the amino group of a second amino acid combine, releasing a water molecule.
The resulting bond is the peptide bond. The products formed by such a linkage are called polypeptides. While the terms polypeptide and protein are sometimes used interchangeably, a polypeptide is technically a polymer of amino acids, whereas the term protein is used for a polypeptide or polypeptides that have combined together, have a distinct shape, and have a unique function.
The Evolutionary Significance of Cytochrome cCytochrome c is an important component of the molecular machinery that harvests energy from glucose. For example, scientists have determined that human cytochrome c contains amino acids.
For each cytochrome c molecule that has been sequenced to date from different organisms, 37 of these amino acids appear in the same position in each cytochrome c. This indicates that all of these organisms are descended from a common ancestor. On comparing the human and chimpanzee protein sequences, no sequence difference was found.
When human and rhesus monkey sequences were compared, a single difference was found in one amino acid. In contrast, human-to-yeast comparisons show a difference in 44 amino acids, suggesting that humans and chimpanzees have a more recent common ancestor than humans and the rhesus monkey, or humans and yeast.
As discussed earlier, the shape of a protein is critical to its function. To understand how the protein gets its final shape or conformation, we need to understand the four levels of protein structure: primary, secondary, tertiary, and quaternary. The unique sequence and number of amino acids in a polypeptide chain is its primary structure. The unique sequence for every protein is ultimately determined by the gene that encodes the protein.
Any change in the gene sequence may lead to a different amino acid being added to the polypeptide chain, causing a change in protein structure and function.
What is most remarkable to consider is that a hemoglobin molecule is made up of two alpha chains and two beta chains that each consist of about amino acids. The molecule, therefore, has about amino acids. The structural difference between a normal hemoglobin molecule and a sickle cell molecule—that dramatically decreases life expectancy in the affected individuals—is a single amino acid of the This can lead to a myriad of serious health problems, such as breathlessness, dizziness, headaches, and abdominal pain for those who have this disease.
Folding patterns resulting from interactions between the non-R group portions of amino acids give rise to the secondary structure of the protein. Both structures are held in shape by hydrogen bonds.
In the alpha helix, the bonds form between every fourth amino acid and cause a twist in the amino acid chain. The R groups are attached to the carbons, and extend above and below the folds of the pleat. The pleated segments align parallel to each other, and hydrogen bonds form between the same pairs of atoms on each of the aligned amino acids.
The unique three-dimensional structure of a polypeptide is known as its tertiary structure. This structure is caused by chemical interactions between various amino acids and regions of the polypeptide. Primarily, the interactions among R groups create the complex three-dimensional tertiary structure of a protein.
There may be ionic bonds formed between R groups on different amino acids, or hydrogen bonding beyond that involved in the secondary structure. When protein folding takes place, the hydrophobic R groups of nonpolar amino acids lay in the interior of the protein, whereas the hydrophilic R groups lay on the outside.
The former types of interactions are also known as hydrophobic interactions. In nature, some proteins are formed from several polypeptides, also known as subunits, and the interaction of these subunits forms the quaternary structure. Weak interactions between the subunits help to stabilize the overall structure. For example, hemoglobin is a combination of four polypeptide subunits. Each protein has its own unique sequence and shape held together by chemical interactions.
If the protein is subject to changes in temperature, pH, or exposure to chemicals, the protein structure may change, losing its shape in what is known as denaturation as discussed earlier. Denaturation is often reversible because the primary structure is preserved if the denaturing agent is removed, allowing the protein to resume its function.
Sometimes denaturation is irreversible, leading to a loss of function. One example of protein denaturation can be seen when an egg is fried or boiled.
The albumin protein in the liquid egg white is denatured when placed in a hot pan, changing from a clear substance to an opaque white substance. Not all proteins are denatured at high temperatures; for instance, bacteria that survive in hot springs have proteins that are adapted to function at those temperatures.
Nucleic acids are key macromolecules in the continuity of life. They carry the genetic blueprint of a cell and carry instructions for the functioning of the cell. DNA is the genetic material found in all living organisms, ranging from single-celled bacteria to multicellular mammals.
The other type of nucleic acid, RNA, is mostly involved in protein synthesis. The DNA molecules never leave the nucleus, but instead use an RNA intermediary to communicate with the rest of the cell. Other types of RNA are also involved in protein synthesis and its regulation.
Each nucleotide is made up of three components: a nitrogenous base, a pentose five-carbon sugar, and a phosphate group. Each nitrogenous base in a nucleotide is attached to a sugar molecule, which is attached to a phosphate group. DNA has a double-helical structure. It is composed of two strands, or polymers, of nucleotides. The strands are formed with bonds between phosphate and sugar groups of adjacent nucleotides.
The alternating sugar and phosphate groups lie on the outside of each strand, forming the backbone of the DNA. The nitrogenous bases are stacked in the interior, like the steps of a staircase, and these bases pair; the pairs are bound to each other by hydrogen bonds. The bases pair in such a way that the distance between the backbones of the two strands is the same all along the molecule.
The rule is that nucleotide A pairs with nucleotide T, and G with C, see section 9. Living things are carbon-based because carbon plays such a prominent role in the chemistry of living things. The four covalent bonding positions of the carbon atom can give rise to a wide diversity of compounds with many functions, accounting for the importance of carbon in living things.
Carbohydrates are a group of macromolecules that are a vital energy source for the cell, provide structural support to many organisms, and can be found on the surface of the cell as receptors or for cell recognition.
Carbohydrates are classified as monosaccharides, disaccharides, and polysaccharides, depending on the number of monomers in the molecule. Lipids are a class of macromolecules that are nonpolar and hydrophobic in nature. Major types include fats and oils, waxes, phospholipids, and steroids. Fats and oils are a stored form of energy and can include triglycerides. Fats and oils are usually made up of fatty acids and glycerol.
Proteins are a class of macromolecules that can perform a diverse range of functions for the cell. They help in metabolism by providing structural support and by acting as enzymes, carriers or as hormones. The building blocks of proteins are amino acids.
Proteins are organized at four levels: primary, secondary, tertiary, and quaternary. Protein shape and function are intricately linked; any change in shape caused by changes in temperature, pH, or chemical exposure may lead to protein denaturation and a loss of function.
Nucleic acids are molecules made up of repeating units of nucleotides that direct cellular activities such as cell division and protein synthesis.
Each nucleotide is made up of a pentose sugar, a nitrogenous base, and a phosphate group. Skip to content Chapter 2: Introduction to the Chemistry of Life.
By the end of this section, you will be able to: Describe the ways in which carbon is critical to life Explain the impact of slight changes in amino acids on organisms Describe the four major types of biological molecules Understand the functions of the four major types of molecules. Figure 2. The underground bulb of camas is baked in a fire pit. In the lock-and-key model, the active site of an enzyme is precisely shaped to hold specific substrates. In the induced-fit model, the active site and substrate don't fit perfectly together; instead, they both alter their shape to connect.
Whatever the case, the reactions that occur accelerate greatly — over a millionfold — once the substrates bind to the active site of the enzyme. The chemical reactions result in a new product or molecule that then separates from the enzyme, which goes on to catalyze other reactions. Here's an example: When the salivary enzyme amylase binds to a starch, it catalyzes hydrolysis the breakdown of a compound due to a reaction with water , resulting in maltose, or malt sugar.
Live Science. Joseph Castro.
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