Biochemistry Essentials
By Jay Templin
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Biochemistry Essentials - Jay Templin
CHAPTER 1
Biological Structure/ Chemistry of Proteins
1.1 Introduction to Biochemistry
1.1.1 What is Biochemistry?
Chemistry is the study of the structure of matter. Matter is anything that has mass and volume. Biochemistry focuses specifically on the molecules of matter, biomolecules, composing living organisms. There are four main classes of important biomolecules: proteins, carbohydrates, lipids, and nucleic acids.
Biochemistry also relates the structure to the function of biomolecules. Starch, for example, is a complex carbohydrate, or polysaccharide. This large molecule consists of many smaller subunits-glucose molecules—which are monosaccharides. When starch is consumed, it is chemically digested into smaller glucose molecules. Glucose, or blood sugar, serves as a source of energy for the estimated 100 trillion cells of the human body.
A knowledge of biochemistry provides an important foundation for understanding all fields of the life sciences, including microbiology and genetics. For example, some antibiotics work by disrupting the protein synthesis machinery of a disease-causing bacterium. DNA is a nucleic acid that encodes the genetic information for the development of an organism’s traits, such as eye color and blood type.
1.1.2 Fields of Biochemistry
The answers to many questions in biology are found at the molecular level. Therefore, other fields that draw on biochemistry include cell biology, zoology, botany, anatomy, physiology, and ecology.
1.2 Polymers/Subunits/Functional Groups
1.2.1 Structure of Polymers
Although many biomolecules are large and complex, they consist of simpler molecules that are bonded together. These smaller molecules are subunits, or building blocks. RNA, for example, is a nucleic acid. This long, chain-like molecule consists of four kinds of simpler subunits, nucleotides, bonded together in the chain.
A polymer is a large molecule consisting of smaller molecules that are bonded together. Among the four classes of biomolecules, examples of polymers and their bonded subunits are as follows:
1.2.2 Functional Groups
There are certain functional groups that form the structure of polymers and their subunits. These functional groups determine the shape and properties of these polymers. An enzyme, for example, is mainly a protein. It must have a specific shape to fit into another molecule and make it reactive. By doing this, an enzyme acts as a catalyst. It speeds up the rate of a chemical reaction.
The structural formulas for some of the major functional groups in biomolecules are shown in Figure 1-1. A structural formula shows the spatial relationship between atoms that are bonded together. Elements, the simplest substances, occur as distinct particles called atoms. All of the basic principles of chemistry apply to biochemistry. Note that the four most common elements in biomolecules are carbon, nitrogen, oxygen, and hydrogen.
Figure 1-1: Structural Formulas of Functional Groups
Atoms unite to form molecules by forming covalent bonds. A covalent bond has one pair of electrons that is shared between the outermost energy shells of two atoms. A carbon atom forms four covalent bonds. Nitrogen forms three bonds, while oxygen forms two and hydrogen forms one.
Some of the major functional groups in biomolecules are as follows:
1.3 Amino Acids—Characteristics and Structure
1.3.1 Structure
Amino acids are the subunits of proteins. Twenty different amino acids commonly occur in living organisms. The general structural formula for an amino acid is shown in Figure 1-2.
The alpha carbon of an amino acid forms four covalent bonds. It bonds to two functional groups—a basic amino group and an acidic carboxyl group. A hydrogen atom is also covalently bonded to this carbon. Amino acids share these three bonded groups in common. However, they differ by the identity of a fourth bonded group, the R group.
Figure 1-2: Structural Formula of an Amino Acid
Figure 1-3: Amino Acid as a Zwitterion
1.3.2 Amino Acids in Water
The R group is different for each amino acid. In the amino acid glycine, for example, the R group is a covalently bonded hydrogen atom. In the amino acid leucine, the R group includes a long carbon chain. For tryptophan, part of the R group is two carbon rings.
The R group of an amino acid can be hydrophilic (water-attracting) or hydrophobic (water-repelling). When dissolved in water, the arrangement of hydrophilic and hydrophobic R groups of bonded amino acids determines the shape of the protein molecule. Hydrophobic groups attract each other and repel water. Hydrophilic groups are often on the surface of a protein structure and orient toward water.
Unbonded amino acids have acid-base properties when dissolved in water. The carboxyl group tends to lose a proton (positively charged) and become negative, a property of acids. The amino group tends to accept a proton and become