Biochemistry Quiz: Carbohydrates and Lipids

A complex sugar molecule that is a major source of energy for the body, especially for the brain. It is measured in blood tests to monitor diabetes.

A type of lipid (fat) that is essential for building cell membranes and producing hormones. It is a key part of metabolic pathways.

The primary protein in blood serum that carries various substances like hormones and drugs. It is often measured to assess liver function and hydration status.

Enzymes are specialized proteins that accelerate biochemical reactions in the body. They are essential for life, acting as biological catalysts.

A group of complex molecules composed of nucleotides that carry genetic information. DNA contains the blueprint for life, while RNA translates this information into proteins.

Series of interconnected chemical reactions within a cell that allow for the synthesis (building up) or breakdown (breaking down) of molecules. These pathways are essential for cellular processes like energy production and repair.

The process of creating complex molecules from simpler ones. It is a part of metabolism and is essential for growth, repair, and energy production.

The sum of all chemical reactions that occur within a living organism. It encompasses both breaking down (catabolism) and building up (anabolism) processes.

A disaccharide composed of glucose and fructose linked by an alpha-1,2 glycosidic bond. It is commonly known as table sugar and is a non-reducing sugar.

A disaccharide composed of glucose and galactose linked by a beta-1,4 glycosidic bond. It is found naturally in milk and is a non-reducing sugar.

A disaccharide composed of two glucose molecules linked by an alpha-1,4 glycosidic bond. It is found in barley, cereal grains, and is a non-reducing sugar.

A type of fatty acid that contains the maximum number of hydrogen atoms. They have no double bonds and are typically solid at room temperature.

A type of fatty acid that contains at least one double bond in its structure. They are typically liquid at room temperature.

A complex carbohydrate made up of many glucose molecules joined together by glycosidic bonds. It is the primary form of energy storage in plants and serves as structural support. The molecule is linear.

A complex carbohydrate made up of many glucose molecules joined together by glycosidic bonds. It is the storage form of glucose in animals and is found primarily in the liver and muscles. The molecule is highly branched.

A complex carbohydrate made up of long chains of glucose molecules joined by glycosidic bonds. It is the primary form of energy storage in plants and found in starch.

A type of lipid composed of three fatty acid chains attached to a glycerol molecule.

A lipid molecule with a hydrophilic (water-loving) head and a hydrophobic (water-fearing) tail. They are crucial for cell membrane structure.

A type of lipid characterized by a structure of four fused carbon rings. They play vital roles in various biological processes.

A type of protein that has a specific three-dimensional shape determined by its amino acid sequence. Proteins carry out a vast array of functions in living organisms.

The basic building blocks of proteins. Each amino acid has a central carbon atom bonded to an amino group, a carboxyl group, a hydrogen atom, and a side chain that varies between amino acids.

The covalent bond that links two amino acids together to form a peptide chain.

A small chain of amino acids linked together by peptide bonds. They are the building units of proteins.

A type of enzyme that catalyzes oxidation-reduction reactions, which involve the transfer of electrons or hydrogen atoms.

A type of enzyme that catalyzes the transfer of a functional group, such as a phosphate group, from one molecule to another.

A type of enzyme that breaks down molecules by adding water. They cleave bonds through hydrolysis.

A type of enzyme that catalyzes the formation of double bonds by either removing or adding a specific group to a molecule.

A type of enzyme involved in various aspects of metabolism, including the breakdown of carbohydrates, lipids, and proteins.

A type of enzyme that catalyzes the rearrangement of atoms within a molecule, changing its shape.

A type of enzyme that joins two molecules together, creating a larger molecule. This process requires energy.

The primary structure of a protein refers to the specific sequence of amino acids in its polypeptide chain, linked together by peptide bonds. This sequence is determined by the genetic code and dictates the protein's unique shape and function.

The secondary structure of a protein refers to the local folding patterns of the polypeptide chain. Common patterns include alpha-helices and beta-sheets, formed by hydrogen bonding between backbone atoms. These structures provide stability and shape.

The tertiary structure of a protein describes the overall three-dimensional shape of a single polypeptide chain. It arises from interactions between amino acid side chains, including hydrogen bonds, ionic interactions, hydrophobic interactions, and disulfide bridges.

The quaternary structure of a protein refers to the arrangement of multiple polypeptide chains (subunits) in a protein complex. These subunits interact through non-covalent bonds, forming a functional unit. Not all proteins have quaternary structure.

Denaturation is a process that disrupts the normal shape of a protein, leading to loss of its function. It can be caused by factors like heat, extreme pH, or chemicals. Denaturation alters the interactions that stabilize the protein's structure.

Peptide bonds are the covalent bonds that link amino acids together in a polypeptide chain. They are formed through a dehydration reaction, where a water molecule is removed.

Proteins play a crucial role in numerous bodily functions. Some examples include storage of essential components like iron, structural support in tissues like hair and bones, acting as catalysts in enzymatic reactions, facilitating muscle movement, transporting various molecules in the bloodstream, and regulating hormones.

The active site of an enzyme contains two specific locations: the buttressing site and the catalytic site. The substrate first binds to the buttressing site, and then the catalytic site causes conformational changes in the enzyme-substrate complex.

Allosteric regulation involves a change in the enzyme's structure due to the binding of a molecule at a site other than the active site. This alteration can either activate or inhibit the enzyme's activity, influencing its function.

Feedback inhibition occurs when the final product of a metabolic pathway inhibits the activity of the first enzyme in that pathway. This process helps regulate the production of the product, preventing an excess.

Proteolytic cleavage is a common way to regulate enzyme activity. It involves the breaking of peptide bonds in the enzyme molecule, either converting an inactive precursor into an active form or permanently inactivating the enzyme.

Competitive inhibition occurs when a molecule that resembles the substrate binds to the enzyme's active site, preventing the substrate from binding and blocking the enzymatic reaction.

Enzymes are used in various medical diagnostic tests. By measuring the activity of specific enzymes in blood or other body fluids, doctors can assess organ function, diagnose diseases, and monitor treatment effectiveness.

Acid phosphatase, alkaline phosphatase, amylase, aspartate aminotransferase, alanine aminotransferase, creatinine kinase, lactate dehydrogenase, and lipase are some enzymes commonly used in medical diagnostics.

Enzymes are used to break down specific molecules in the body, catalyzing various reactions. They are essential for vital processes like digestion, energy production, and DNA replication.