Learning Journal Unit 1

Comparing Covalent and Ionic Bonds

Understanding covalent and ionic bonds is essential to comprehending chemical interactions. The

way electrons are shared or moved between atoms is where they fundamentally diverge.

Ionic bonds

When electrons are fully transported from one atom to another, these bonds are created. As a

result, ions with opposing charges are created when one atom acquires electrons (anion) while the other

loses them (cation). An ionic bond is created when these oppositely charged ions are drawn to one

another.

For example, sodium gives an electron to chlorine to produce sodium chloride (NaCl), which is kept

together by electrostatic attraction.

Covalent Bonds

On the other hand, covalent bonds are created when atoms share electrons in order to form a

configuration that is more stable. A molecule is made up of atoms that share one or more pairs of

electrons to complete their outer electron shells.

For instance, four hydrogen atoms and carbon share electrons in a methane (CH4) molecule to form a

tetrahedral structure that is bound together by covalent bonds.

These linkages affect a substance's characteristics and are essential to the synthesis of many chemicals

that are present in biological systems.

 Van der Waals interactions and hydrogen bonds are important in cells.

Hydrogen bonds play a critical role in preserving the structural integrity of biological molecules.

The double helix structure of DNA is maintained by hydrogen bonding between complementary base

pairs, adenine-thymine and guanine-cytosine. The genetic information contained in DNA would be

vulnerable without these connections.

Furthermore, hydrogen bonding has a major role in the structure of proteins. They maintain

secondary structures (beta sheets and alpha helices) and folding patterns that are critical to a protein's

ability to function. Enzymes, for example, efficiently catalyze biological reactions by virtue of the exact

structures they retain through hydrogen bonding.

Van der Waals Interactions

Transient variations in the distribution of electrons within molecules produce relatively weak

interactions known as Van der Waals forces. Large macromolecules like proteins depend on them to

preserve their three-dimensional structure in spite of their weakness.

Protein folding and stability are facilitated by these interactions, which enable proper protein

function. The binding of molecules like enzymes to their substrates is influenced by van der Waals forces,

which also affect enzymatic activity in cells.

Three Vital Components in Biological Molecules Aside from Carbon:

Despite being the most basic element,

1. Hydrogen (H)
 Hydrogen (H) is found in many biological compounds. It is the building block of organic molecules

such as proteins, lipids, carbohydrates, and nucleic acids. It forms covalent connections with carbon,

oxygen, nitrogen, and other elements. For example, hydrogen atoms are bound to carbon and oxygen

atoms in glucose, a carbohydrate, which contributes to its structure.

2. Oxygen (O):

The process through which cells produce energy by breaking down glucose in the presence of oxygen

is known as cellular respiration, and oxygen (O) is necessary for this activity. Water molecules,

carbohydrates, lipids, and nucleic acids like DNA and RNA are examples of biomolecules that contain

oxygen atoms in their structure.

3. Nitrogen (N):

Amino acids, which are the building blocks of proteins, contain nitrogen (N), an essential ingredient.

Together with DNA and RNA, it is a part of nucleic acids. In the end, peptide bonds—which establish the

structure and functionality of proteins—are formed between amino acids by nitrogen atoms alone.

In conclusion, the interactions between various types of chemical bonds and the presence of elements

beyond carbon are vital for the structure, stability, and function of biological molecules, forming the basis

of life's complexity and diversity.

References

McMurry, John. "Chemistry." Pearson Education, Inc., 2011.

Alberts, Bruce, et al. "Molecular Biology of the Cell." 4th edition, Garland Science, 2002.

Lehninger, Albert L., et al. "Lehninger Principles of Biochemistry." 7th edition, W. H. Freeman, 2017.

Berg, Jeremy M., et al. "Biochemistry." 7th edition, W. H. Freeman, 2010.

Nelson, David L., and Cox, Michael M. "Lehninger Principles of Biochemistry." 6th edition, W. H.

Freeman, 2013.