AP Bio: Chemistry of Life

Carbon

- it has four valence electrons - It can form up to four covalent bonds - all organic compounds contain this

Polypeptide

long chain of amino acids that makes proteins

Oxidation

losing an electron

Transport Proteins

membrane proteins that help move substances across a cell membrane

isomers

molecules that have the same molecular formula but differ int heir arrangement of these atoms

Peptide Bond

The covalent bond between the amino acids

Inorganic Compounds

compounds that do not cotain carbon

Central Dogma

DNA is rewritten as RNA which is then used to make proteins

Protons

positively charged particles found in the nucleus of the atom, never changes

Trace elements

elements required by an organism but only in minute quantities

Covalent Bond

- A covalent bond forms when electrons between atoms are shared, which means that neither atom completely retains possession of the electrons, the electronegativiteis are similar

Ionic Bond & Ions

- An ionic bond forms between two atoms when one or more electrons are TRANFERRED from one atom to the other. - The two atoms must have very different electronegativities - The atom that gains the electron has an overall negative charge and is called an anion - The atom that loses the electron has an overall positive charge and is called a cation - Example NaCl - ion: charged atom or molecule

Hydrogen Bonds

- Bonds that are weak bonds between molecules. - form when a positively charged hydrogen atom in one covalently bonded molecule is attracted to a negatively charged area of another covalently bonded molecule.

Nonpolar Covalent Bond

- electrons are shared equally - the electronegativies are equal meaning they are both able to pull electrons the same (O2)

Polar Covalent Bond

- electrons are shared unequally - electronegativies are different, and an unequal distribution of the electrons result - the electrons forming the bond are closer tot he atom with the greater electronegativity and produce a negative charge or pole near the atom - the weaker pull produces a positive pole (H2O)

Why Enzymes denature at high temperatures, or wrong pHs?

- Enzymes are proteins, meaning that they are strings of amino acids connected together by peptide bonds that form a certain structure. Proteins have several different structures in how they may exist - primary, secondary, tertiary, and quaternary. The primary structure of a protein is just the linear sequence of amino acids. The secondary structure involves hydrogen bonding between amino acids. The tertiary structure involves bonding between R-groups and the quaternary structure usually involves multiple protein interactions. Denaturing at high temperatures occurs because high temperatures rupture some of the bonding that occurs in these quaternary/tertiary/and secondary protein structures. Once these bonds are broken, the enzyme (protein) is reduced to its primary structure with just peptide bonds occurring - the functional structure of the enzyme is lost and it is no longer functional. This works for most proteins. In the case of the enzyme, however, when the structure is lost, the active site and allosteric site also lose their functionality and therefore no substrate may bind to the enzyme - H ions have a positive charge which means that they are attracted to the negative parts of certain molecules (or negative ions).An enzymes tertiary structure is held in place by a number of ionic and hydrogen bonds. These bonds help to ensure that the active site of the enzyme is held in the right shape. These bonds occur because of the attraction between oppositly charged groups on the amino acids that make up the enzyme protein.Because of the charge of the H+ ions, they are able to interfere with the hydrogen bonds and the ionic bonds that are holding the enzymes tertiary structurre in place. This means that increasing or decreasing the concentration of hydrogen ions in a soluition around an enzyme ( changing the pH of the solution) can alter the tertiary structure of the enzyme molecule. So changes in pH can also cause changes to the shape of the active site, therefore denaturing it.

Why do hydrogen bonds cause high specific heat? Also include why water has a high heat of vaporization

- Much of the heat absorbed by water is used to break hydrogen bonds. Only a small amount of heat is left over to increase molecular motion. Since temperature measures molecular motion, the temperature rises only slightly. Molecules that don't make hydrogen bonds, like CO2, attract each other more weakly, so a larger fraction of absorbed heat can raise the temperature. Also each water molecule can make up to 4 hydrogen bonds - Boiling occurs when all the water molecules have so much energy that their motions break most of the hydrogen bonds. Then the liquid rapidly changes to gas bubbles (steam). If you keep adding heat to boiling water, the temperature stays the same because all the heat is used to break hydrogen bonds. The free molecules (steam) carry away energy.

Explain the difference between saturated fatty acids, monounsaturated fatty acids, and polyunsaturated fatty acids.

- Unsaturated cys: Hydrogens are on the same side, liquids, plants, typically healthier, double bond - Unsaturated trans: Hydrogens are on opposite sides, bad, still double bond - Monounsaturated/polyunsaturated: 1 double covalent bond/2 or more double covalent bonds - Saturated Fatty Acid: single double bond, each carbon is "saturated" with hydrogen, higher melting temps, solid at room temps. - The double bond in a fatty acid creates a bend at the bond which slightly spreads the triglyceride apart, so that's why they are a liquid at room temperature - Saturated fatty acids tend to be packed together more tightly

Dehydration Synthesis/Condensation Reaction

A chemical reaction in which two molecules covalently bond to each other with the removal of a water molecule. (two monasaccharides connect to form a disaccharide)

Competitive inhibition

A competitive inhibitor has a structure that is so similar to the substrate that it can bond to the enzyme just like the substrate

A nucleic acid molecule has a distinct 3' end and a 5' end. In one or two sentences explain the significance of these ends during the assembly of a double-helix DNA molecule

A double helix DNA molecule consists of two single-strands of DNA. The base paring between nucleotides requires that the two strands are arranged in opposite directions, or anti parallel. So to achieve this one strand is arranged from the 3 prime end to the 5 prime end and the other strand is arranged from the 5 prime end to the 3 prime end.

solution

A homogeneous mixture of two or more substances (solvent + solute)

Monosaccharide and examples

A monosaccharide is the simplest kind of carbohydrate. It consists of a simple sugar molecule like glucose or fructose and have the formula (CH2O)2

Noncompetitive Inhibitor

A noncompetitive inhibitor binds to a site on the enzyme that is not the active site

Quaternary Structure

A protein that is assembled from two or more separate peptide chains. The bonds that occur in tertiary structure are also present in this. An example of this would be hemoglobin (so like the shirt and pants)

Compound

A substance that is made up of atoms of two or more different elements joined by chemical bonds

ATP

Adenosine triphosphate (ATP) is the high-energy form of adenosine because it contains the most phosphate groups (three). This molecule fuels many different endergonic (energy-requiring) enzymatic processes in biological organisms. ATP molecules diffuse or are transported to the place where the energy is needed and deliver chemical energy from the breaking of their phosphate bonds

Monomer for Proteins, Carbohydrates, and Nucleic Acids, and Lipids

Amino Acids, monosaccharide Nucleotides, Lipids don't really haven official one but triglyceride

Describe how allosteric enzymes work, include allosteric effector, allosteric activator, allosteric inhibitor, and feedback inhibitor.

An alltosteric effector is something that binds to the enzyme on an allosteric site, not the active site. An allosteric activator binds to the enzyme and induces the enzyme's active form. An alosteric inhibitor binds to the enzyme and induces the enzyme's inactive form. In feedback inhibition an end product of a series of reactions act as an allosteric inhibitor shutting down one of the enzymes.

Cooperativity

An enzyme becomes more receptive to additional substrate molecules after one substrate molecule attaches to an active site. This occurs for example in enzymes with two or more sub units like hemoglobin.

Denatured

An enzyme is denatured when it loses its native conformation and its biological activity, irreversible

Cells are mostly made of water. In one or two sentences explain why the specific heat of water is important to a cell

Because water has a high specific heat capacity, its temperature changes very slowly in response to energy changes. As a result, metabolic activities occurring in the cell that release or absorb energy do not significantly change the temperature of the cell, allowing the internal temperature of the cell to remain fairly constant, which is important in maintaining homeostasis and cell functions that life depends on.

Explain the significance of temperature and the presence of an enzyme on the rate of a reaction

Both temperature and the presence of an enzyme increase the rate of a reaction. Because molecules are moving faster at higher temperatures there are more collisions and therefore more reactions. As a catalyst an enzyme speeds up reactions by facilitating the coming together of the reactants (thus lowering activation energy). At 45 degrees Celsius, the influence of the enzyme is eliminated because the high temperature denatures it and the reaction rate falls back to the rate that occurs in the absence of an enzyme.

How do Enzymes speed up Reactions

By: - binding two substrates in the active site, which provides the correct orientation for them to react to form a product - using a co factor that interacts with the substrate to facilitate the reaction - binding the substrate to the active site, which can stretch bonds in the substrate that need to be broken - by providing a microenviornment with a different pH in the active site to help facilitate the reaction

Six Elements essential to Life

C, H, O, N, P, S (Carbon, hydrogen, oxygen, nitrogen, phosphorous, sulfur they make up about 96% of living matter)

Polysaccharides

Carbohydrates (sugar) that consists of a series of connected Monosaccharides. Some examples of Polysccharides include:

Describe the role of cofactors in chemical reactions, include coenzymes and inorganic cofactors.

Cofactors are nonprotein molecules that assist enzymes like metal ions. Coenzymes are organic cofactors that usually function to donate or accept some compoonent of a reaction, often electrons. They bind to an enzyme and plays a role in catalysis. Coenzymes contain carbon. Help by increasing the rate.

Complex Carbohydrates vs. Simple Carbohydrates

Complex Carbohydrates are important for energy and storage

DNA vs. RNA

DNA: - longer - double helix - deoxyribose - stays in nucleus - paired by weak hydrogen bonds between the bases, to form the double strand - 5 (phosphate group attached to the fifth carbon of the deoxyribose) to the 3 carbon, the other segment is anti parallel starting at the 3 prime end and ending at the 5 RNA: - RNA is made by copying short segments of DNA, so DNA is longer than RNA - RNA can be a double helix but it is not common - ribose - leaves the nucleus - uracil not thymine

What are bi products of cellular respiration?

Heat, Carbon DIoxide, and Water

Structure determines _________

Function

The Functional Groups

Functional groups are organic mmolecules that share properties because they have similar clusters of atoms. The ones we have to know include hydroxyl, carboxyl, amino, phosphate, and methyl

Activation Energy

In order for a chemical reaction to take place, the reacting molecules must first collide and have sufficient energy to trigger the formation of new bonds

Irreversible Inhibtor

Irreversible inhibitor forms a covalent bond with an amino acid side group within the active site, which prevents the substrate from entering the active site or prevents catalytic activity.

Hydrolysis:

One molecule is split to form two seperate molecules by the addition of water

Describe the role of ATP in metabolic reactions.

It releases energy when a hydrolysis reaction breaks the last phosphate bond of the ATP molecule to form DP and an inorganic phosphate group. It contains adenosine, a sugar and 3 phosphate groups

Lipids

Lipids are a types of macro molecule that are not soluble in water but are highly soluble in non polar substances. The The most common examples of lipids are fats, oils, phospholipids, and steroids.The monomer for lipids are triglycerides

The different Macromolecules and function of each

Macromolecule = large molecules - Carbohydrate: Energy, energy storage, structural - Important energy source, insulation, phospholipids of plasma membrane - Proteins: enzymes; movement; membrane receptors - Nucleic Acids: Heredity; code for amino acid sequence

Metabolism, catabolism, synthesis or anabolism

Metabolism are chemical reactions that occur in biological systems. It includes the break down of substances which is catabolism, and the formation of new products which is synthesis or anabolism

Nucleotides (include structure)

Monomer for DNA, it consists of a nitrogen base, a five-carbon sugar called deoxyribose, and a phosphate group. There four DNA nucleotide, each with one of the four nitrogen bases: Adenine, Guanine, Thymine (Uracil), and Cytosine

polymer and monomer

Most macro molecules are polymers molecules that consist of a single monomer unit repeated many times.

Hydrophobic

Non polar substances that do not dissolve in water are hydrophobic. These substances include oils

List the order of bonds in water from strongest to weakest

Nonpolar covalent Polar Covalent Ionic Hydrogen Van Der Waals

Protein

Polymers of amino acids covalently bonded.

Why carbon atoms are so versatile, and why that is important to life?

Since carbon atoms are tetravalent, or are able to form four bonds, atoms may branch off a carbon atom in as many as four places. The ability of a carbon atom to form four different bonds allows carbon to form many different sizes and types of molecules. They can form chains, rings, or combinations of chains and rings.

Atom

Smallest unit of an element

Describe the structure and function of starch, cellulose and glycogen, and chitin

Starch: a polymer of a-glucose molecules. It is the principal energy storage molecule in plant cells. We can easily digest (break apart the bonds) this Cellulose: a polymer of a-glucose molecules. It differs from starch by its pattern of polymer branching. It is a major component of plant cell wals Glycogen is a b-glucose molecule. It is a storage polysaccharide found in animals , veterbrate muscle cells, and liver cells Chitin: a polymer similar to cellulose, but each B-glucose molecule has a nitrogen containing group attached to the ring. Chitin serves s a structural molecule in the walls of fungus cells and in the exoskeletons of insects other arthropods

Steroid (typical structure and function)

Steroids are characterized by a backbone of four linked carbon rings. Some examples of steroids include cholesterol, hormones like testosterone and estrogen. They also act as messengers

Storage Proteins

Storage of amino acid such as ovalbumin in egg whites, and zein in corn seeds

Hydrophilic

Substances that dissolve water are considered water loving. These include ionic compounds, polar molecules, and some proteins

Glycosidic Bonds/Linkage

The bond that binds sugars

Equilibrium

The condition where the rate of reaction in the forward direction equals the rate of reaction in the reverse direction and as a result there is no net production of reactants or products.

Nucleic Acids

The genetic information of a cell is stored in molecules of deoxyribonucleic acid (DNA). The DNA, in turn passes its genetic instructions to ribonucleic acid (RNA) for directing various for directing various metabolic activities of the cell.

Purines

The number of purines equals the number of pyrimidine, longer and fatter, Adenine and Guanine (pure silver, a double-ring base

Cohesion

attraction between like substances, occurs in water because of the hydrogen bonding that occurs between water molecules

Tertiary Structure

The structure of the tertiary structure includes additional three-dimensional shaping and often dominates the structure of globular proteins. It is dependent on the many stabilizing forces due to bonding interactions between the side-chain groups of the amino acids. Some bonds include - Hydrogen Bonding between R groups of amino acids - Ionic Bonding between R groups of amino acids - Hydrophobic Bonding two hydrophobic R groups move toward the center of the protein - Disulfide Bonds a very strong bond that occurs when the sulfur atom in the amino acid cysteins bonds to another sulfur atom in another cystein. Helps in maintaining the folds of the amino acid chains.

Describe and explain the significance to life, the following properties that water has do to hydrogen bonding: a. ice is less dense than water b. cohesion c. adhesion d. capillary action e. heat capacity f. universal solvent g. high surface tension

The structure of water is the key to its special propeties. Water is made up one atom of oxygen and two atoms of hydrogen, bonded to a form a molecule - - Ice: The openings in the lattice make ice less dense than liquid water, so it floats. That causes water to freeze from the top down, so there's always liquid in which organisms can live. Ice floats because of the weakness of hydrogen bonds. This weakness allows hydrogen bonds to constantly break and reform, allowing molecules to periodically approach one another in the liquid state. In the solid state the hydrogen bonds become rigid and form of a crystal that keeps the molecules separated and less dense. This keeps larger bodies of water from freezing solid, allowing life to exist in ponds, lakes, and even oceans - Cohesion is allowed to happen because of hydrogen bonding, and it contributes to a high surface tension, creating a water surface that is firm enough to allow many insects to walk upon it without sinking, also enables plants to transport water from the roots to the leaves against the force of gravity. It is the linking of like molecules - Adhesion: Water is transported in plants through both cohesive and adhesive forces; these forces pull water and the dissolved minerals from the roots to the leaves and other parts of the plant. - Capillary Action: Adhesion is observed when water "climbs" up the tube placed in a glass of water: notice that the water appears to be higher on the sides of the tube than in the middle. This is because the water molecules are attracted to the charged glass walls of the capillary more than they are to each other and therefore adhere to it. This type of adhesion is called capillary action. It also allows water to move through plant roots and stems and the smallest blood vessels in your body - as one molecule moves up the tree root or through the capillary, it 'pulls' the others with it. - Heat capacity: moderation of temperature is possible because of water's high specific heat. The amount of heat required to raise or lower the temperature of a substance by 1 degrees celsius. Water has a high specific heat because the hdyrogen bonds between the water molecules must be ddisrupted to raise the temperature. water must lose a large amount of heat and form many additional hydrogen bonds for its temperature to decreatse. This allows our bodies to maintain homeostasis, and Eath's oceans to be relatively stable. - Universal Solvent: Water is considered the universal solvent because it can dissolve a lot of things. Ionic substances are soluble in water because the poles of the polar water molecules interact with the ionic substances and separate them into ions. Substances with polar covalent bonds are similarly soluble because of the interaction of their poles with those of water - surface tension: Because of the hydrogen bonding, water molecules are strongly attracted to one another, which gives water a high surface tension. The molecules at the surface of the water "stick together" to form a type of 'skin' on the water, strong enough to support very light objects. Insects that walk on water are taking advantage of this surface tension. Surface tension causes water to clump in drops rather than spreading out in a thin layer.

Phospholipids

They look almost like the Triglycerides except that one of the fatty acid chains is replaced by a phosphate group (-PO3^2-). An R group is covalently attached to the phosphate group and create the hydrophilic and polar head. The two fatty acid tails are non polar and hydrophobic. They help in cell membranes.

Secondary Structure

Three dimensional shape that results from the hydrogen bonding between the amino and carboxyl groups of adjacent amino acids. The bonding produces a spiral (alpha helix) or a folded plane that (beta pleated sheet). (The crisscrossing of threads in clothes)

Triglyceride

Triglycerides include fats and oils. They consist of three fatty acids attached to a glycerol molecule. They are used for storage of energy

Disaccharide

Two or more sugar molecules joined by a glycosidic linkage. During the linkage a water molecule is lost

How come when you sweat you feel cool?

Water has a high specific heat meaning in order to change the temperature water you must add a large amount of energy to warm (boil) or remove a large amount of energy to cool (and freeze) water. This is because a lot of the energy is used to break apart/reestablish hydrogen bonds. So when you sweat, a large amount of heat is taken with it.

Explain why water is a polar molecule, include partial charges both negative and positive.

Water molecules are polar, becasue the oxygen region of the molecule has a partial negative charge and each hydrogen has a partial positive charge.

Why don't polar molecules and nonpolar molecules mix?

Water molecules cling to one another and won't part to make room for uncharged (nonpolar) molecules. Also there is no attraction or repulsion between polar and non polar things.

The protein albumin that surrounds the yolk of an egg is a clear liquid when raw and a white solid when cooked. In one or two sentences, explain why cooking causes this change

When a protein is heated above a critical temperature, it begins to lose its three-dimensional structure. When the secondary, tertiary, and Quaternary structure of a protein break down, as they will when there is excessive heat like in cooking, the structure of the protein is permanently destroyed, as evident by the changing of the clear liquid to a white solid.

The process of cellular respiration, which converts simple sugars such as glucose into CO2 and water, is an example of _____.

a catabolic pathway

Elements

a substance that cannot be broken down to other substances by chemical reactions

a) Describe why phospholipids are important components of cell membranes, based on their structure and properties. b) Explain why proteins are an important component of the cell membrane, based on their structure and properties.

a.) A phospholipid molecule contains a hydrophilic "head" and two hydrophobic fatty acid tails. In cell membranes, surfaces, phospholipids are arranged in a bilayer in which the hydrophilic heads are in contact with the cell's watery interior and exterior whereas the tails are pointed away from water and toward each other in the interior of the membrane. The fatty acid chains of phospholipids can contain double bonds which make them unsaturated. Because of the kinks in the tails, phospholipids aren't packed together tightly, which contributes tot he fluidity of the membrane. The fluidity of the cell membrane is very important in its function; the less fluid the membrane is, the more impermeable it is. There is an optimum permeability for the cell membrane at which all the substances necessary for metabolism can pass into and out of the cell. The fluidity of cell membranes enables hydrophobic molecules such as hydrocarbons, carbon dioxide, and oxygen to dissolve in the bilayer and easily cross teh membrane. However, ions and polar molecules (including water, glucose, and other sugars) cannot readily pass through because of the hydrophobic interior. Protein channels and transport proteins allow these required substances to cross membranes 2.) There are numerous functions of proteins in the membrane. One important function is tahat some proteins protrude on the extracellular side of the membrane and serve as receptors for signaling molecules. A second function is seen with proteins that extend through the interior of the bilayer and serve as channels for the passage of molecules or ions that cannot pass through the phospholipids.

Catalyst

accelerates the rate of reaction by lowering the activation energy required for the reaction to take place. It is any substance that accelerates a reaction but does not undergo a chemical change itself. So an enzyme is a type of catalyst.

What is the difference between acidity and alkalinity?

acidity = acid alkanity = base

Amino Acids

amino acids are linked by a peptide bond. This is why a protein polymer is often called a polypeptide. Structure: They contain a amino group, a R group, an H, and carboxylic acid. The R group in amino acids is what makes them unique. They are called acids because they contain carboxyl groups in their backbone.

Free Energy

amount of energy that can be used in a chemical reaction

Buffers

are substances that minimize changes in pH. They accept H+ from solution when they are in excess and donate H+ when they are depleted. Buffering compounds are essential in living tissues to minimize pH changes

Amino (draw on whiteboard)

behaves as bases, they are polar, and are hydrophilic, they can accept protons from solution

Carbohydrate

carbohydrates are the most abundant class of biolmolecules on Earth, and most of this biomass is produced through photosynthesis

Keto (draw on whiteboard, carbonyl)

carbonyl group is located in the center of the chain

Aldehyde (draw on whiteboard, carbonyl)

carbonyl located at the end of the chain named by replacing al with e. e.g. butanal

Structure of Amino Acids

carboxyl group, a central carbon with a hydrogen, R group, and amino group

Organic Compounds

contain carbon atoms, large organic molecules are called macromolecules

Chemical Bonds

interactions between the valence electrons of different atoms.

Endergonic Reaction

energy is gained, positive g

Exogonic Reaction

energy is released, negative g

Heat energy has the highest amount of _________ of any kind of energy

entropy or disorder

Chemical bonds

form because of the interaction of valence electrons

Sulfhydrl (draw on whiteboard, thiol)

forms disulfide bonds, polar, neutral pH, hydrophilic, helps in formation of tertiary structure (thiols), and can form a permanent link in proteins

Isotopes

forms of an element with differing numbers of neutrons.

Reduction

gaining an electron

Molecules

groups of two or more atoms that are held together by chemical bonds

Acidic

have an excess of H+ ions and a pH below 7.0 [H+] > [OH-]

Basic

have an excess of OH= ions and pH above 7.0 [H+] < [OH-]

Defensive Proteins

help provide protection against foreign substances that enter the bodies of animals like antibodies

Hydroxyl (draw on whiteboard)

highly polar and may act as a weak acid, alchohOL, can bind with water molecules and other electronegative molecules

Electrons

negatively charged particles that are found in the electron shells around the nucleus. They determine the chemical properties and reactivity of the element.

Can an enzyme extract heat from the environment?

no

Neutral

pH of 7 [H+] = [OH-]

Neutrons

particles with no charge. They are found in the nucleus

Phosphate ( draw on whiteboard)

polar, hydrophilic, acid. They provide major energy Some examples are DNA, ATP, and phospholipids

The lower the activiation energy the more. . . and the faster. . .

product formed per unit time and the faster the reaction rate

Atomic Number

protons

Atomic Mass

protons + neutrons, bigger number

Hydrogen Bond

relatively weak bonds that form between the partial positively charged hydrogen atom of one molecule and the strongly electronegative oxygen or nitrogen of another molecule.

Pyrmidines

single-ring nitrogen bases, smaller and skinnier, Thymine & Cytosine

solute

substance that dissolves in water

Electronegativity

the ability of an atom to attract electrons, plays a large part in determining the kind of bond that forms.

Describe the function of enzymes, include the terms substrate, induced-fit model, active site. Are enzymes changed as a result of a reaction? What affects the efficiency of an enzyme? Also Describe the structure of enzymes and how they are regulated

the active site is where the substrate attaches to the enzyme As the substrate enters the active site, the enzyme changes shape slightly due to interactions between the substrate's chemical groups and chemical groups on the side chains of the amino acids that form the active site. This shape change makes the active site fit even more snugly around the substrate. This induced fit is like a clasping handshake. Enzymes regulate the rate of chemical reactions Enzymes are globular proteins that act as catalysts (activators or accelerators) for metabolic reaction. an enzyme is considered a catalyst because it speeds up chemical reactions without being used up. They are also considered specific because of their ability to recognize the shape of a particular molecule. An enzyme is unchanged as a result of a reaction. The efficiency of the enzyme is affected by temperature and pH. The induced fit model describes how enzymes work. Within the protein (the enzyme) there is an active site with which the reactants readily interact because of the shape polarity or the other characteristics of the active site.

solvent

the one that's doing the dissolving

Primary Strucuture

the order of amino acids attached to each other. The bond in this covalent peptide bond, thread in clothes, is the basis of proteins

pH scale

the pH scale runs between 0 and 14 and measures the relative acidity and alkalinity of aqueous solutions

Substrate

the reactant in a catalyzed reaction so the substance or substances that the enzyme acts upon

aqueous solution

the solution when the solvent is water

Methyl (draw on whiteboard)

they are non polar, and hydrophobic. They help in the formation of the lipid bilayers and protein folding. Some include fatty acids, oils, and waxes

The difference between Alpha Glucose and Beta Glucose

they differ simply by a reversal of the H and OH on the first carbon (first one clockwise after O). Alpha has H on top and OH on bottom, and Beta has OH on top and H on bottom

Structural Proteins

used for support such as connective tissue and keratin that forms hair and finger nails

Carboxyl (draw on whiteboard)

usually acts as an acid, they are polar and hydrophilic. Some examples include acetic acid, amino acids, fatty acids, and sugars

Van der Waal forces

very weak forces that are the result of asymmetrical distribution of electrons within a molecule

Hydrolysis

water is added to split larger molecules.