Biology- Biomolecules and water quiz

Cohesion

When water molecules are attracted to each other.

Adhesion

When water molecules are attracted to other surfaces.

Capillarity

Movement of a liquid through a porous material (material with a bunch of holes)

Covalent bonds

Sharing of electrons between two non mentals

Ionic bonds

The transferring of electrons between a non-metal and a metal

Specific heat capacity

-The amount of heat that must be added to one unit of mass of the substance in order to cause an increase of one unit in temperature

-Helps moderate earths temperature

hydrogen bonding

-adhesive strength

-Capillarity

-cohesive

hydrolysis

Chemical breakdown of a compound due to reaction with water

Polymer

-Any class of natural or synthetic substances composed of very large molecules, called macromolecules. Ex: proteins, cellulose, nucleic acids.

-Water is removed in order to make a polymer

-To break a polymer it has to go through hydrolysis

fatty acids

-Any of a class of organic compounds that are fatty acids or their derivatives and are insoluble in water but soluble in organic solvents. They include many natural oils, waxes, and steroids.

-Nonpolar covalent bonds

-Long term energy (because they have more carbons they contain more energy)

-C, H, O

-Stored energy turns into ATP

-Unsaturated fatty acid= polar

-Saturated fatty acid= non-polar

-Marcomolecule

Animo acids

-R chain

-Amine group

-Carboxylic acid group

-C, H, O, N, S

-20 common amino acids—> each has a different side group represented by the R group

Nucleic acids

-Nitrogen base

-Sugar

-Phosphate group

-C, H, O, N, P

-Genetic material

-Macromolecule

Carbohydrate

-Short term energy (important source of energy)

-C, H, O

-Macromolecule

-For every carbon there is a water molecule

-Most end in “ose”

Protein

-Made of amino acids

-Carbon in the center (surrounded)

-Variable R side chain (this is the only thing that differs in each protien)

-Amine group (NH2)

-Carboxylic acid group (COOH)

-Amino acids linked by peptide bonds

-Body building

-Macromolecule

-

Glucose (C6H12O6)

-Monosaccharide

-simple sugar

-Carbohydrate

Saccharides (sugar)

-Made up of C, H, O

-Carbohydrates

Monosaccharides

-Simple sugar (Glucose (C6H12O6) & fructose)

-Simplest carbohydrate

Phospholipid

-Essential fat-like molecules forming cell membranes, they form a protective lipid bilayer that controls what enters and exits a cell

-Structurally similar to fats but only contain 2 fatty acids attached to a glycerol

Monomer

-A monomer is a small molecule that can chemically bond with other similar molecules to form a much larger molecule, called a polymer.

Triglyceride

-Triglycerides are a type of fat (lipid) in your blood, the most common form of fat in your body, serving as a key energy source by storing extra calories from food, sugar, and alcohol, and releasing them for energy when needed.

Least likely compound to dissolve in water?

-Non-polar fats & oils (lipids) compounds

Why does ice float on liquid?

-Because ice is less dense than water

Which types of compounds dissolve easily in water?

-Ionic & polar compounds

Crystallized solid

When the molecules freeze, there is a specific pattern.

Non-polar

-CH group

-hydrophobic

-On the inside (afraid of the water)

-Equal sharing

Polar

-OH

-Hydrophilic

-On the outside

-Stronger attraction, allowing for it to attract other atoms easier

-Unequal sharing

Myoglobin

-Found in the skeletal muscle

-Binds to oxygen

-Made up of Alpha helix’s and Oxygen

Amine group

-Part of proteins/amino acids

-NH2

Carboxylic acid group

-COOH

-

Transport protein

Cell membrane, oxygen does in, carbon dioxide gets sent out (waste)

Structural protein

Muscles are made of proteins

Dehydration synthesis

-Water is taken away in order to bind amino acids

Secondary structure

-Alpha helix (spiral)

-Beta pleated (folded)

-Hydrogen bonds

Primary structures/polypeptide chain

-Peptide bonds

-amino acids bonded together

Tertiary structure

-Hydrophilic bonds

-Hydrophobic bonds

-Hydrogen bonds

-Ionic bonds

-Disulphide bridge

Hydrophilic bond

-Polar

-OH

-Outside

Hydrophobic

-Non polar

-Inside

-CH

R group/side chain

-Chemical properties

-Physical properties

Water

-Helps synthesize molecules

-Make & break

-Vector that helps facilitate chemical reactions

-Help maintain life forms through cooling the earth (water cycle)

-Solvent of life

Enzyme

-A protein that helps with chemical reactions in the body

-Macromolecule

Disaccharide

-two monomers

-O-glycosidic bonds

-Sucrose is the most common disaccharide

-Two monosaccharides linked by a glycosidic bond

-Hydrocarbons are bonded differently

-C12H22O11

Polysaccharides

-Macromolecule

-monosaccharides linked together (more than 2)

-EX: starch, cellulose, chitin

Hydrophobic

-Afraid of water

Unsaturated fatty acid

-Fatty acid whose hydrocarbon chain contains more than one double bond

Saturated fatty acid

-no double bond in its hydrocarbon chain

Steroids

-Lipids that contain four fused rings

-multiple rings of carbon atoms linked together

Quaternary structure

-4 identical polypeptide chains come together and form a functional protein complex

-highest level of protein organization

Chemical reactions

-breaking existing chemical bonds and creating new ones

Hydrogen bonds

-Make water cohesive

-Moderate temperature

What is the primary reason that protein folding is essential for protein function?

Folding creates the correct 3D shape that allows the protein to perform its specific biological role

Which level of protein structure describes the sequence of amino acids held together by peptide bonds?

Primary structure

 

What type of chemical bonds are primarily responsible for the formation of alpha helices and beta pleated sheets in secondary structure?

Hydrogen bonds

How do hydrophobic and hydrophilic R groups influence protein folding during tertiary structure formation?

Hydrophilic R groups tend to be on the outside near water; hydrophobic R groups tend to be on the inside away from water

 

What is the relationship between genes and the primary structure of a protein?

Genes made of DNA determine the order and number of amino acids in a protein

 

In quaternary structure, what holds multiple polypeptide chains together as subunits?

Hydrogen bonds and disulfide bonds

 

What role do chaperonins play in protein folding?

They provide an ideal environment inside their barrel-shaped structure to help proteins fold correctly

 

How can a single change in one amino acid affect a protein's function

The amino acid sequence is critical to protein structure and function, so even one change can alter how the protein works

 

What is denaturation and what can cause it

Denaturation is the disruption of a protein's shape due to exposure to conditions outside its ideal temperature or pH range

Which of the following interactions are involved in tertiary structure formation?

Ionic bonds, Van der Waals interactions, disulfide bonds, and hydrogen bonds involving R groups