Biochemistry Basics Quiz

<p>Carbonyl group (C=O) (D)</p> Signup and view all the answers

<p>Hydrolysis reaction (A)</p> Signup and view all the answers

<p>Fructose (A), Ribose (C)</p> Signup and view all the answers

<p>α 1-2 (D)</p> Signup and view all the answers

<p>Maltose (C)</p> Signup and view all the answers

<p>They always consist of a single type of monosaccharide. (C)</p> Signup and view all the answers

<p>Starch is composed of amylose and amylopectin. (E)</p> Signup and view all the answers

<p>Amino acids are the monomers that make up proteins. (C)</p> Signup and view all the answers

<p>They are typically referred to as oils. (B)</p> Signup and view all the answers

<p>Oleic acid is a monounsaturated fatty acid, and it contains one carbon-carbon double bond. (B)</p> Signup and view all the answers

<p>Cis fatty acids have a kink in the chain, while trans fatty acids have a straight chain, and trans fats can be created through processing. (B)</p> Signup and view all the answers

<p>They are required by the body but cannot be synthesized, so they must be obtained through diet. (D)</p> Signup and view all the answers

<p>To act as insulation and prevent water from sticking to surfaces. (C)</p> Signup and view all the answers

<p>Phospholipids contain a modified phosphate group, while other lipids do not. (C)</p> Signup and view all the answers

<p>They form a barrier that separates the intracellular and extracellular environments. (C)</p> Signup and view all the answers

<p>Steroids contain a closed ring structure, while other lipids have a linear structure. (A)</p> Signup and view all the answers

<p>It is the unique sequence of amino acids in a polypeptide. (C)</p> Signup and view all the answers

<p>It can lead to a change in protein structure and function. (C)</p> Signup and view all the answers

<p>A change in the nucleotide sequence of the DNA that codes for the protein. (B)</p> Signup and view all the answers

<p>The presence of a different amino acid at position seven in the beta chain. (D)</p> Signup and view all the answers

<p>Hydrogen bonding (A)</p> Signup and view all the answers

<p>To determine the sequence of amino acids in the protein. (D)</p> Signup and view all the answers

<p>It can alter the amino acid sequence and therefore the structure and function of the protein. (A)</p> Signup and view all the answers

<p>All of the above (D)</p> Signup and view all the answers

<p>The side chains of certain amino acids favor the hydrogen bonding patterns found in alpha-helix structures, while others prefer the patterns found in beta-pleated sheets. (D)</p> Signup and view all the answers

<p>Disulfide bonds formed between the carboxyl groups of amino acids. (B)</p> Signup and view all the answers

<p>Weak, non-covalent interactions between the polypeptide subunits, such as hydrogen bonding and van der Waals forces. (A)</p> Signup and view all the answers

<p>An increase in the temperature of the solution to a high enough level. (B)</p> Signup and view all the answers

<p>Tertiary structure refers to the arrangement of amino acids in the polypeptide chain, while quaternary structure is about the interactions between multiple polypeptide chains. (B)</p> Signup and view all the answers

<p>Hydrogen bonds stabilize both secondary and tertiary protein structures. (A)</p> Signup and view all the answers

<p>Denaturation can lead to a temporary or permanent loss of function, depending on the protein and the denaturing conditions. (B)</p> Signup and view all the answers

<p>Secondary structure is formed by interactions between the side chains of amino acids. (B)</p> Signup and view all the answers

Biological molecules that speed up chemical reactions.

A reaction that forms new bonds and requires energy.

A reaction that breaks bonds and releases energy.

The simplest carbohydrates, usually with 3-7 carbons, ending in -ose.

Carbohydrates have the formula (CH2O)n, with a 1:2:1 ratio of C:H:O.

A monosaccharide found in fruits and part of sucrose.

Monosaccharides exist as linear chain or ring-shaped molecules.

Disaccharides form when two monosaccharides link through a dehydration reaction.

A covalent bond formed between monosaccharides in disaccharides and polysaccharides.

Long chains of monosaccharides linked by glycosidic linkages, can be branched or unbranched.

Fats without carbon-carbon double bonds, usually solid at room temperature.

Fats that contain one or more carbon-carbon double bonds in their chain.

A type of unsaturated fat with one double bond in its carbon chain.

A type of unsaturated fat containing more than one double bond.

Hydrogens on the same side of the chain in unsaturated fats.

Hydrogens on opposite sides of the chain in unsaturated fats.

Fatty acids required by the body but not produced by it, must be consumed in the diet.

Molecules with two fatty acids and a phosphate group, crucial for cell membranes.

Substances that do not mix well with water.

A common steroid synthesized in the liver and precursor to hormones and vitamin D.

The most abundant organic molecules with diverse functions including regulatory and structural roles.

The building blocks of proteins, consisting of an α-carbon, amino group, and side chain.

Varied side chains in amino acids that determine their chemical properties.

Amino acids that must be obtained through diet.

A bond formed between two amino acids during dehydration synthesis.

Enzymes that break down substrates into simpler molecules.

Enzymes that build more complex molecules from simpler ones.

A chain of amino acids joined together by peptide bonds.

The unique sequence of amino acids in a polypeptide, determining its identity.

The process where a gene's information determines the amino acid sequence of a protein.

A condition caused by a single amino acid change in hemoglobin leading to abnormal cell shape.

Local folding of a polypeptide, including formations such as α-helix and β-sheet.

A common secondary structure formed by hydrogen bonds, resembling a spiral staircase.

The overall 3D shape of a polypeptide, determined by interactions between side chains.

A secondary protein structure formed by hydrogen bonds between backbone atoms.

Forces that drive hydrophobic R-groups to cluster inside the protein structure.

The structure formed by the association of multiple polypeptide chains into a single protein.

The process by which a protein loses its structure and function due to environmental changes.

Covalent bonds formed between cysteine side chains that help stabilize protein structure.

Chemical interactions between R-groups of amino acids that influence protein folding.