Proteins are large biomolecules consisting of long chains of amino acids.* Proteins, also called polypeptides, are macromolecules composed of *amino acids, largely containing carbon, hydrogen, oxygen, and nitrogen. Individual amino acids are bonded together by a *peptide bond. Proteins differ from one another primarily in the sequence of their amino acids. Proteins are made on ribosomes using the genetic code contained in DNA. Protein structure is dictated by the nucleotide sequence of their genes which usually results in the protein folding into a specific 3D structure that determines its function. With proteins, *shape is important. The specific shape of the protein determines its function. They are the *work horses of the cell, performing a vast array of functions within organisms, including: catalyzing metabolic reactions, DNA replication, responding to stimuli, providing structure to cells and organisms, and transporting molecules from one location to another. Some of the most important proteins in organisms are *enzymes which serve as biological catalysts in metabolic pathways.* The arrangement and quantity of amino acids affect the structure and function of that protein. Remember, *structure determines function. *Primary structure refers to the sequence of amino acids joined by peptide bonds. Fredrick Sanger discovered the first protein amino acid sequence for insulin in 1948. Primary Sequence is very important. This is where mutations often change the structure of the protein and thus, its function. Consider the difference between sickled cells and normal red blood cells. The only difference in the two is a change from glutamic acid to valine in the sixth position in the primary sequence. This one difference in amino acids causes Sickle Cell disease. *Secondary structure is created by hydrogen bonds between neighboring amino acids which allows for overlapping and coiling to occur. These help fold the protein into it’s unique shape and allows for flexibility. The repeating patterns of the secondary structure include the alpha helix and the beta pleated shapes. Denaturing occurs when the unraveling of a protein or enzyme causes it not to function. It can be caused by ph changes, solution changes, and temperature changes. The most common bonds affected when proteins are denatured are the weak hydrogen bonds associated with its secondary structure. *Tertiary structure is a 3D folding pattern of the protein due to interactions between R groups in one amino acid chain. These interactions include ionic bonds, hydrogen bonds, hydrophobic interactions, and disulfide bridges formed between R groups of amino acids. Lastly, the *quaternary structure is the association of two or more polypeptide chains into one large protein, such as hemoglobin. Any change in any level of protein structure may result in a change in the protein function.*

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Question 1
Proteins are one of the four main types of _________ .
Responses
A biomoleculesbiomolecules
B livingliving
C complexcomplex
Question 2
One of the main functions of proteins is the creation of ________.
Responses
A sugarssugars
B enzymesenzymes
Question 3
Enzymes are important for allowing and speeding up ________ in an organism.
Responses
A reactionsreactions
B chemicalschemicals

Answer all 3 questions only using the provided responces

Question 1: A - biomolecules

Question 2: B - enzymes
Question 3: A - reactions