Macromolecules: Proteins, Carbohydrates, and Lipids

What are the four main types of macromolecules that characterize living things?

What type of smaller molecules covalently bond to construct polymers?

What is the name of a reaction that produces water and joins monomers to create a polymer?

What is the name of the process to break down macromolecules?

How many different amino acids are found in proteins?

What are carbohydrate monomers called?

What are the four kinds of molecules that form nucleic acids?

Give an example of a molecule containing a hydroxyl functional group.

What property is conferred to a molecule with a hydroxyl group?

The aldehyde functional group is very reactive and important in building molecules because it releases what?

What property is associated with the aldehyde functional group?

What functional group, important in carbohydrates and energy reactions, has the structure C=O bonded to two carbon atoms?

In living tissues, the carboxyl functional group ionizes and acts as what?

What functional group accepts H+ in living tissues and acts as a base?

What is released when a phosphate group is bonded to another phosphate?

What functional group stabilizes protein structure by forming disulfide bridges?

What functional group is nonpolar and important in energy transfer?

What term describes unbranched polymers of covalently bonded amino acids?

What type of isomers are amino acids?

What is the function of the side chains (R groups) of amino acids?

Which amino acids have electrically charged side chains at pH levels typical of living cells?

Name three amino acids with polar but uncharged side chains.

In what type of solution do amino acids with nonpolar hydrocarbon side chains cluster together?

List the three special case amino acids.

What is the name given to the covalent bond formed when two cysteine side chains react in an oxidation reaction?

What characteristic of glycine allows proteins to be flexible at its location?

What structural feature does proline lack that significantly limits its ability to participate in hydrogen bonding?

What are short polymers of less than 20 amino acids called?

Linking of amino acids involves a dehydration reaction between what two groups attached to the alpha carbon?

Distinguish between the impacts of moderate heat, and extreme heat, on protein confirmation.

What is the definitive 3D arrangement of a protein?

What name is given to the process of a protein unfolding and losing its native conformation?

What level of protein structure results from the ways in which subunits bind together and interact?

What chemical feature of a protein must exist for a molecule to bind to it?

What is the general formula for carbohydrates?

What are the four major biochemical roles of carbohydrates?

Name one important structural polysaccharide found in plant cell walls?

Besides cellulose, what other polysaccharide is composed of glucose?

Lipids are characterized by what property?

Name three types of lipids and their role in living organisms.

Name the four major types of molecules that characterize living things.

What type of chemical reaction links monomers together to form polymers?

What are the unbranched (linear) polymers of covalently bonded amino acids called?

What determines the unique three-dimensional shape of each polypeptide chain?

What is the difference between fats and oils at room temperature, and what accounts for this difference?

What term describes molecules, like phospholipids, that have both hydrophilic and hydrophobic regions?

What is the role of chaperones in protein folding?

What are the primary functions of structural proteins?

Describe the impact of high concentrations of polar or nonpolar substances on protein structure.

Describe the role of R-groups in determining the properties of amino acids.

What is the role of gene regulatory proteins?

Why are lipids not considered true polymers?

What type of bonds stabilize the secondary structure of proteins?

How could a mutation altering a single amino acid within a protein disrupt its function, even if the overall structure appears unchanged?

Describe a scenario where hydrolysis is crucial in dismantling a polysaccharide. Which specific bond is broken, and what happens to the water molecule?

Imagine a newly discovered organism thrives in extremely cold environments. Hypothesize how its membrane phospholipid composition might differ from typical organisms.

Consider a protein domain consisting primarily of hydrophobic amino acids. Predict its location within a soluble, globular protein in an aqueous cellular environment. How would this arrangement affect protein function?

A scientist successfully synthesizes a novel artificial amino acid with a side chain containing a heavy metal ion coordinated to several nitrogen atoms. If incorporated into a protein, how might this amino acid's unique properties be exploited for biotechnological applications (consider protein purification, drug delivery or novel catalysis)?