Exam 1 Worksheet Short Answers Flashcards
(125 cards)
Describe the difference between an ionic bond and a covalent bond
In an ionic bond, one atom has given up one or more electrons, leaving it with a positive charge, while the other atom has taken on one or more electrons, leaving it with a negative charge. The attraction between the oppositely charged cation and anion create the ionic bond.
A covalent bond is formed when two atoms share electrons, creating a stronger and more stable bond.
How is a hydrogen bond formed?
When one atom has a hydrogen atom covalently bound to another atom that exerts a stronger pull on the shared electrons, this creates a polar covalent bond. The hydrogen atom in the bond has a slight positive charge (delta +), and it will be attracted to other molecules with slight negative (delta -) atoms or to outright negatively charged atoms. Thus, the hydrogen bond is a weak bond formed by attractions of opposites, similar to an ionic bond, but weaker because the hydrogen atom involved is not fully + charged.
Explain why ions interact easily with water.
Water molecules are formed by polar covalent bonds between an oxygen and each of its two hydrogen partners. The hydrogen atoms are thus each delta +, and available to hydrogen bond with any negatively charged atoms (anions). The oxygen atom of a water molecule has a delta2- charge and will be attracted to any positively charged atom (ie: cations). Thus, all ions have electrical attractions to water molecules: anions to the delta+ hydrogen end of the water molecule, cations to the delta 2- oxygen end of the water molecule.
A neutral solution would have a pH of
7
The pH of blood is normally in what range?
7.35-7.45
A solution with a pH of 12 is
basic
A solution with a pH of 2 is
acidic
a solution of pH 5 has ___ times ___ hydrogen ions than a solution of pH 2
1000
fewer
How would 100-fold decrease in pH affect an enzyme that normally functions at neutral pH?
Most enzymes are proteins, and every protein functions best at a certain pH and temperature. For most proteins, this optimum pH is close to blood pH, and this optimum temperature is close to normal body temperature. As pH conditions move away from that ideal, the bonds holding the protein in its optimum shape are affected, causing the protein to bend or unfold into a different shape. Since a protein’s function is dependent on its shape, altered protein shape leads to altered protein (in this case, enzyme) function
What is the relationship between an enzyme and the activation energy for a chemical reaction
Most chemical reactions in the human body would not take place at body temperature or pH. In other words, it is improbable for two substrates to come together on their own simply by contact. But when an enzyme binds the substrates, it alters their shape enough so that they can bind with one another. The enzyme essentially lowers the energy (the “activation energy”) required for them to interact. Once a reaction has occurred between the substrates, the new product leaves the enzyme. The enzyme then returns to its original shape and is available to catalyze another reaction.
Based on what you know about the electron shell model of carbon, explain why carbon forms the backbone of so many organic molecules
Carbon has an atomic number of 6, so in the electron shell model would have 4 electrons in its second shell. This atom is stable with 8 electrons in that second shell, so carbon can share pairs of electrons with one, two, three or four other atoms, including other carbon atoms. This leaves carbon as a main building block of a wide variety of organic compounds, of all lengths and branching patterns
Why are carbohydrates considered to be “hydrated carbon”?
Most carbohydrate molecules are built with carbon atoms that have a hydrogen and an OH group as two of its bonding partners
Name the four classes of organic molecules
Carbohydrates, lipids, proteins, and nucleic acids
Carbohydrates:
Its building block - monosaccharides (and disaccharides)
Whether it is hydrophilic or hydrophobic - hydrophilic
The most common forms of the molecule in the body- glucose and its storage form glycogen are important energy molecules; other polysaccharides are found within cells and in extracellular space
Proteins:
Its building block amino acids
Whether it is hydrophilic or hydrophobic most proteins as a whole are hydrophilic, though within a protein there can be stretches of amino acids that are hydrophobic
The most common forms of the molecule in the body : membrane proteins, enzymes, structural proteins, signaling proteins – there is no end to the classes of important proteins we will find in the human body
lipids
Its building block fatty acids, glycerol, cholesterol
Whether it is hydrophilic or hydrophobic generally hydrophobic; phospholipids (which are amphipathic) are an important class of lipids with one end hydrophobic and the other hydrophilic
The most common forms of the molecule in the body: cholesterol, phospholipids, fatty acids, glycerol, triglycerides, steroid hormones
nucleic acids
Its building block deoxyribonucleotides, ribonucleotides
Whether it is hydrophilic or hydrophobic hydrophilic
The most common forms of the molecule in the body DNA, RNA, ATP
What is meant by the primary structure of a protein? Secondary? Tertiary? Quaternary?
The primary structure simply describes the linear sequence of amino acids in the protein
The secondary structure occurs when amino acids in the primary structure form hydrogen bonds with neighboring amino acids, causing the protein to bend or fold into an alpha helix or a pleated sheet shape
The tertiary structure occurs when amino acids find new neighbors after the protein twisted into its secondary shape; new bonds form and alter the shape into its final form. For most proteins, the tertiary structure is its final shape, and the protein has some function for the body in this final shape.
The quaternary shape of a protein is when one or more proteins, each in their tertiary shape, bind together to form a new conglomerate protein. Each protein part of this bigger protein is now referred to as a protein subunit of the final protein. Usually the tertiary proteins that come together here are not functional on their own – they must form the complex quaternary structure protein to have a function. Only some proteins in the body have a quaternary structure
Why are temperature and pH important factors in protein function?
Every protein functions best at a certain pH and temperature. For most proteins, this optimum pH is close to blood pH, and this optimum temperature is close to normal body temperature. As pH conditions move away from that ideal, the bonds holding the protein in its optimum shape are affected, causing the protein to bend or unfold into a different shape. Since a protein’s function is dependent on its shape, altered protein shape leads to altered protein function.
The four bases used in RNA molecules are
guanine, cytosine, adenine, and uracil
The four bases used in DNA molecules are
guanine, cytosine, adenine, and thymine
What are some key differences between RNA and DNA molecules?
The sugar molecule used in the nucleotide (ribose in RNA, deoxyribose in DNA)
RNA is single stranded, DNA is double stranded
RNA moves from the nucleus to the cytoplasm, DNA stays in the nucleus (there is also some DNA in mitochondria, which we will not talk about in this course)
How is the structure of an ATP molecule related to its function in the body?
ATP is an adenosine nucleotide (adenine base off a sugar-phosphate unit) with two additional phosphates, making for 3 total phosphates (“triphosphate”). The terminal phosphate is cleaved, leaving an ADP molecule (adenosine diphosphate), a phosphate, and the energy liberated from the bond which can now power cell reactions.
the building blocks of carbohydrates are
monosaccharides