Biology Exam 1

pH

- hydrogen ion concentration - Above 7 is basic and below 7 is acidic.

van der Waals forces

- a slight attraction that develops between the oppositely charged regions of nearby molecules

Monomer

- A simple compound whose molecules can join together to form polymers - A very generic term that can apply to different things - Example: Glucose is a monomer specifically a monosaccharide that can create polymers or polysaccharides such as starch, glycogen, and cellulose. - Cannot be bridged by transient connections but rather covalent bonds because you dont want them to break apart but rather provide structure to create a polymer.

Proportions of Macromolecules within Living Organisms

- Bulk of the cell is water (70%) - Rest of the Cell is built up by macromolecules. (*Note that lipids cannot be considered macromolecules but are rather large biological molecules because they cannot polymerize which is associated with macromolecules) . - Among the macromolecules, Proteins take up the most space and this is understandable because Proteins perform a diverse range of functions for the cell. They help in metabolism by providing structural support and by acting as enzymes, carriers, or hormones. After Proteins, Nucleic Acids are the next most abundant macromolecule because it holds the instructions required for proteins. Then comes Sugars and finally lipids.

Noncovalent bonds

- Intermolecular. - LDFs, D-D, H- bonds, and ionic bonds. (van der waals) - These are bonds between two or more molecules. - Very weak so that they can be easily broken. Weak bonds are effective because they contribute to the emergent properties of life. The reversibility of weak bonds can allow two molecules to come together, do their business and then separate.

Covalent Bonds

- Intramolecular - Bonds created by sharing electrons with other atoms. - Examples: Disulfide bridges, peptide bonds, phosphodiester linkages, glycosidic bonds - Polar covalent and nonpolar covalent

RNA What are difference between RNA and DNA in terms of the sugar and type of nitrogenous bases that are there?

- It also uses hydrogen bonding. Wraps around itself don't always exist in a linear fashion. - Normally exists as a single strand, but can fold upon itself and connect through hydrogen bonds.

Sickle Cell Disease How does the form change impact function? Where do we look for change? If Glutamine is located at 6th amino acid which terminus is it located in C or N terminus?

- Modification in the primary structure. (DNA level change) Changes Glutamic Acid in the 6th Amino Acid to Valine. Changes amino acid side chain from polar to nonpolar and because a red blood cell exists in the aqueous environment it's gonna try and shift and contort itself to minimize its exposure with the environment. This morphs the structure to become a sickle to avoid interaction with the aqueous solution. - Single substitution impacting protein sequence impacting protein function. - Deforms red blood cells and impacts its jobs. A little sticky causes agglutination which means clumps of them together and this increases the risk of blood clots and less oxygen. Changing amino acids won't always cause a significant impact. - Swapping polar with something else that's polar it probably won't change anything. - LOOK AT SHIFT OF PROPERTY!!!!

Ionic Bonds

- Type of noncovalent bond. -Between Cations (+) and Anions(-) and involves transfer of electrons - Salts // Ionic Compounds

Hydrogen Bonding

- the intermolecular force in which a hydrogen atom that is bonded to a highly electronegative atom is attracted to an unshared pair of electrons of an electronegative atom in a nearby molecule. - Hydrogen covalently bonds to N, O, F. This is still a noncovalent interaction even though the bonds are covalent.

Chaperones

-Proteins that assist in protein folding during post-translational processing. -Places protein in an optimal state - Proteins may behave inappropriately after synthesis, but chaperones sequester it and provide the right environment. - Not all proteins depend on chaperone. - Not enzymes just another type of proton - Are present right after the primary structure.

Diversity of Carbon

-The diversity of Carbon can be seen by the many forms that a carbon skeletal can take. The carbon skeleton can differ in length, positions of double bonds, branching, and the presence of rings. - Know that these diversifications occur because Carbon has 4 valance electrons.

Emergent properties of water

1. Cohesive behavior ( Water to Water) - Surface tension. The measure of how difficult it is to stretch or break the surface of a liquid due to cohesion (ex. a spider walking on the water surface) 2. Ability to moderate temperature ( Retain its temperature in spite of temperature changes around it like on a beach the sand gets hot but the water stays cool) Water has a very high specific heat, therefore a lot of energy is required to increase its temperature 3. Expansion upon freezing ( With the creation of Ice density decreases) 4. Versatility as a solvent (Universal solvent) 5. Acts as an acid/base buffer. Water can form up to 4 hydrogen bonds. When it is in the ice state then it has to have 4 hydrogen bonds. However, when it is in 3 or 4 it can be liquid. For gass there are no hydrogen bonds between the water molecules. (Test Question)

Cholesterol

A lipid that forms an essential component of animal cell membranes and acts as a precursor molecule for the synthesis of other biologically important steroids. Decreases fluidity within the membrane at moderate room temperatures. Increases fluidity at lower temperatures. Molecules will usually slow down because of the interaction of van der waals forces between hydrocarbons, but putting in the cholesterol it prevents this interaction and prevents freezing and increases the fluidity. Slight changes in shape can cause large changes in function.

Electronegativity

A measure of the ability of an atom in a chemical compound to attract electrons

Nucleotides : Sugar

A pentose (5 carbons) - 2' carbon. Either you can have a hydroxyl group or a hydrogen group. If it is a hydroxyl group then we have a and we will use this sugar to create RNA. If we have a hydrogen group then we have a deoxyribonucleic acid which will be apart of DNA. - 1' use for N glycosidic bond to link nitrogenous base to sugar. - 5' used to link the phosphate group. - 3' used to polymerize nucleotides by joining to 5' phosphate group.

hypertonic solution plasmolyzes plants and shrivels animals

A solution in which the concentration of solutes is greater than that of the cell that resides in the solution

Hypotonic solution (Normal for Plants and is called turgid) bad for animal cells because they become lysed.

A solution in which the concentration of solutes is less than that of the cell that resides in the solution

Similarities / Differences between Active vs Passive transport

Active goes from Low Concentration to High Concentration (against the concentration gradient) and requires ATP. Passive Transport goes from high concentration to low concentration (spontaneously) and requires no energy, because it is going down the concentration gradient. Both use ion channels to move ions across the cell membrane, in or out of the cell. (Are channels involved in active transport or is it only carriers?) active transport does NOT use channels because it needs a binding event to occur and phosphorylation, thus carrier proteins ARE used to transport ions in active transport. Channel and carrier proteins can be used in passive transport, and energy is not needed.

Classification of Amino Acids

Amino Acids are classified by their side chains. aka grouped based on their r group. Hydrophobic - Nonpolar side chains Hydrophilic - Polar side chains / Charged side chains. (these will be attracted to water but will also attract opposite charged) Negatively Charged Side Chain = Acidic Positively Charged Chain = Basic Cysteine contains sulfhydryl functional group, Cysteine is only weakly polar so classify it as polar but remember it's only slightly polar. Sulfhydryl groups form disulfide bridges with one another through an oxidation reaction.

Transmembrane Proteins

Any part of the protein that is inserted into the membrane is an integral Any part of the protein that is not inserted but is loosely associated with the membrane. A little inside is integral. WHole thing inside is transmembrane and loose attachment is peripheral. Polypeptide backbone is polar. But R GROUP is what determines its category and function. Most of time it is Alpha helices (nonpolar R groups) forming barrels within membrane to tuck polarity inside. Can have beta sheets

Primary Structure of Protein You have the first amino acid to form a polypeptide chain, which component of this amino acid is responsible for facilitation elongation? Does the R group play a role in this structure?

Based on the amino acid sequence of the polypeptide chain. Categorized by the R group. Formed through covalent peptide bonds. EXCLUSIVELY COVALENT Answer: Carboxyl End Answer: R group plays no role until the tertiary structure

Fatty Acids

Carboxyl Group(red) attached to hydrocarbon tails of various lengths. - Carboxyl group makes it an acid - A different number of covalent bonds present.

Amino Acid structure (Monomer for Protein) Are Amino Acids Amphipathic ( Having polar and non-polar characteristics)

Central carbon atom Amino group (Basic because it accepts H) Carboxyl group (Acidic because it donates H) Single hydrogen Variable R group (Sidechain) ONLY R GROUP CHANGES EVERYTHING ELSE CONSIDERED BACKBONE.

How are subunits/monomers bridged together to form polymers?

Condensation/dehydration synthesis is used to bridge subunits together. Use of covalent bonding indicated by solid lines. A - B. This is not achieved by simply putting them next to each other but rather are driven by other things. Just having water won't work. Using enzymes to facilitate is one way. - Sugar into tea. Placing macromolecule into an aqueous solution. It has ode hydroxyl groups and is polar so it loves water. You expect the sugar to dissolve become homogeneous. The sugar isn't being hydrolyzed. Rather because sugar exists as a crystalline structure you'll have a bunch of sucrose molecules connected through noncovalent bonds and what you're hoping for is that water will disturb sugars noncovalent bonds and not the smaller covalent bonds. You're not chemically changing the sugar.

Functional Groups

Determines Properties of Organic Molecules.

Breaking down large macromolecules to form

Different shapes can be broken down to much smaller components and synthesized to function the human body in many ways

Triglycerides (Fats)

Fatty Acid IS NOT A Fat. In order to create Triglycerides, there need to be three fatty acids and one glycerol molecule. Fat synthesis occurs through condensation reaction where the hydroxyl portion of the carboxyl group in your fatty acid and the hydrogen from the hydroxyl group of your glycerol will be removed and this will cause the creation of an Ester linkage. (Covalent bond) THIS HAPPENS 3 TIMES These covalent bonds are a great way to store energy.

FLIP

Fluorescence loss in photobleaching. In this one, the Lazer is left on. A continuous stream of photobleaching. The cell gets progressively lighter until no more fluorescence. We still have lateral diffusion but as soon as it pulls up to the sight of interest it gets blasted and loses fluorescence. Eventually, the entire thing becomes bleached.

FRAP Can it fully recover? What if membrane wasn't dynamic?

Fluorescence recovery after photobleaching Photobleaching is the application of light at a certain frequency to destroy ONLY fluorescence. Once it is photobleached it is gone for good. Lazer turned off after one shot. -At first, we see completely bleached. But with enough time we see a recovery of fluorescence. We see this recovery because membrane proteins found outside of the bleached area move via lateral diffusion into the previously bleached area. Colored ones are migrating into the area of interest. - The graph shows a significant drop indicating successful fluorescence. The height can reach the same height of the original recovery if everything in the area of interest over time becomes completely replaced.

Membrane Fluidity Heterocaryon Experiment. Think bout experimental modifications... Time Temperature Why are you looking at membrane proteins and not the actual membrane?

Forming of the fused cell. - Heterocaryon means the two nuclei are different from one another. - Notice that the antibody structures are different for each. - They use antibodies to emit a certain color. They are also specific to the cell. - Wherever you see red you see human protein and wherever you see green you see mouse protein. - If a membrane is not dynamic you would see half green and half red. - If it is dynamic then you would expect to mix after enough time. Oscillation of colors. You see movement because they have moved from their original placement. - We look at protein to conclude theories about membranes. We cannot track phospholipids because of the diversity of R groups. We cannot track phospholipids also because antibodies cant be conjugated to lipids only proteins.

Nucleotides : Nitrogenous Base

G with C (3 hydrogen bonds) A with T (2 hydrogen bonds) Purines (2 rings) - Adenine (RNA and DNA) - Guanine (RNA and DNA) Pyrimidines (Single ring) - Cytosine - Both (RNA and DNA) - Thymine - DNA - Uracil - RNA

Phospholipid Structure

Glycerol + 2 fatty acids + phosphate group + POLAR - R group (Sidechains). Dont worry about how this affects functions.

Phospholipid Activity

Hydrophobic and Hydrophilic. Amphipathic Maximizes like-like interactions and minimizes, unlike interactions. This is done by making the hydrophilic heads face towards the aqueous solution and have hydrophobic tails face each other. This is done through the creation of a bilayer. Usually, you will see on tail saturated and the other unsaturated. Micelles are formed by Fatty acids.

Membrane Permeability

Hydrophobic small goes in easily. hydrophobic big goes in but has a tough time. Small uncharged polar like H20 some goes in but not all because polar. Large polar barely have any chance because its polar and big. Charged ions never go through by themselves because they are attracted to hydrophilic head are rejected by hydrophobic / nonpolar bilayer. Ions would have to go through large nonpolar area which is very uncomfortable. They need a chanel protein.

Secondary Structure of Protein How many options do you have for the secondary structure of a protein? What kind of noncovalent bonds is taking place in this structure? Is the R group involved here? If I have 2 beta-pleated sheets what level of protein have I achieved?

In the secondary structure, we now build upon the primary structure by adding on hydrogen bonds. (in the backbone) You have 2 options - Alpha helices (Organized turns within single strand ) - Beta pleated sheets (If you have more than one polypeptide it is possible for 2 polypeptides to interact in beta-pleated sheets) (In this case it becomes Quaternary) Hydrogen bonding between hydrogen and oxygen. A protein usually has both alpha helices and beta-pleated sheets in secondary structure don't have to be exclusively one.

Storing Energy When you make bonds you normally release energy so how come when ester linkages or glycosidic bonds form they store energy?

It absorbs energy because it breaks certain bonds before making new ones through a condensation reaction. It also releases more energy when being formed. Therefore it's still an overall exothermic reaction

Do all channel proteins have a hydrophilic channel?

It depends on what they are transporting across the membrane.They def all have hydrophobic outsides so that they can be inside the hydrophobic core but the inside part depends on what type of molecule the channel is transporting. Channel proteins are sometimes available for large, uncharged (hydrophobic) molecules that require assistance to pass through the cellular membrane. NOT ALL channel proteins will have a hydrophilic channel. It is false to assume that all channel proteins will have a hydrophilic core.

Membrane Fluidity can be affected by?

Length and double bonds of phospholipids.

What occurs in the oligopeptide? Label the hydrophobic and Hydrophilic How would expect this to behave in a nonpolar solution or really any solvent? What would its general goal be?

Like with Like// For overall chemical behavior. Protein Categorization is very ambiguous, but can be described as largely polar or largely non polar. This means that there can be a mix of residues but there will be more residues of one certain type between hydrophobic and hydrophilic. Minimizing exposure for unfavorable conditions.

Functions of Lipids

Lipids overall have hydrophobic properties. - Cell signaling (Hormones) - Energy Storage (Bonds) - Temperature control (Insulation source for metabolism generating heat for metabolism) -Protection - what can get in or out of cell. (Regulation) - Structure / Stability Lipids cannot be polymerized but can still have condensation reactions but cannot continue to add on lipids to whatever length is desired, NOT MCROMOLECULE

Tertiary Structure of Protein. If I have two Cysteines in my polypeptide chain can I absolutely form disulfide bridges?

Look at side chains of Amino acids to stabilize the protein in this level Covalent bonds can be seen in this level because of cysteine residues that contain sulfhydryl groups. Covalent bond (disulfide bridges) can only be formed if there are two Cysteines (which means two sulfhydryl groups). THEY REQUIRE CLOSE PROXIMITY The majority of bonds are noncovalent. These are all transient and are easily breakable so not really stabilizing structure compared to disulfide bridges. Hydrophobic Interaction we are thinking about egregious pushed together by the environment. Pushing hydrophobic together to avoid interacting with an aqueous solution. van der Waals, not the same as hydrophobic and occur due to slight dipole interactions. There are hydrogen bonds, Ionic bonds, hydrophobic interactions, and van der Waals. These are all caused by close proximity and are dependant upon the side chain of the amino acid. Everything in terms of stabilization and bonds depends on the kind of amino acids. It doesn't HAVE to happen.

The Cell Membrane as a Fluid Mosaic

Membrane Movement / Fluidity - Goes through lateral diffusion - side to side movement on the same side - Rotation in place or rotation and lateral movements. - A flip flop is very rare because the Roles of the membrane between intracellular and extracellular are different.

Similarities / Differences between Micelle vs phospholipid bilayer

Micelles occur when you have fatty acids (one tail) while phospholipid bilayers will form when you have phospholipids (two tails) because they take up more space. Both occur in the presence of an aqueous or polar environment.(Does it always have to be polar? Can it be non-polar?) The hydrophobic tails aggregate away from the polar environment via hydrophobic interactions and the polar head groups interact with the polar environment. Fatty acids form micelles while phospholipids form bilayers. Micelle formation occurs instead of bilayer formation due to the single fatty acids being able to more compactly squeezed in than the two fatty acid chains on the phospholipid.

Organism based diversity

Organism based diversity is caused by diversification in the order of which our macromolecules are arranged. An example would be DNA and the way its different in terms of order.

Membrane Potential With Ions

Outside membrane is positive and inside is negative so protons have easy time moving to negative side, however negative ions have a tougher time.

Monomer - Macromolecules - Macromolecular Assemblies Why do we want Non-covalent bonds when constructing a higher level of structure like a ribosome when we know that building a larger structure requires covalent bonding. ?

Monomers are usually characterized by covalent bonds to form macromolecules and macromolecules mainly utilize non-covalent bonds to form macromolecular assemblies. This does not mean that there are no covalent bonds when forming macromolecular assemblies. Answer: The behavior of certain macromolecular assemblies that need to associate and dissociate readily. I have covalent bonds that need a lot of energy to dissociate readily. A ribosome's job is to associate and disassociate ode within a cell in order to achieve its job it wants to be as efficient as possible. - Cellular efficiency.

Cell Mmembrane

Primarily composed of Lipids// Phospholipids. It also contains proteins. It contains Sugars that could be bound to proteins. The diversity of molecules means form leads to function. Examples include signaling membranes. Membrane = Fluid Mosaic. There is membrane movement or fluidity

Protein's Roles

Protein's Roles - Enzymatic Breakdown: Amylase - Defense: Integral role in the Immune system. - Serve as Storage: can be hydrolyzed for energy. - Transport: Facilitating movement - Hormones - Receptors ( Cell to Cell communications) - Support Ode diversity in jobs so we can expect diversity of structure. Structure determines backbones.

Protein Stability / Denaturing a Protein -What happens to a denatured protein? -In which cases can a denatured protein be renatured? -If a polypeptide chain is hydrolized what would happen to it? - What kind of experiment would you design to prove protein renaturation? How would you know its denatured and how would you know its renatured?.

Proteins a be disrupted by a number of external stress factors including temperature, pH, removal of water, presence of hydrophobic surfaces, presence of metal ions and high shear. The loss of secondary, tertiary or quaternary structure due to exposure to a stress factor is called denaturation. -Change in pH can disrupt the pattern of ionization which can expose carboxyl or amino groups and disrupt electrostatic attractions or repulsion. Impact on Ionic bonding. This can affect tertiary or quaternary. -Increasing/decreasing temperature can change the rate of molecular collision whether its increasing or decreasing. Impact on hydrogen bonds presenting themselves. Close proximity bonds won't be able to be maintained if it's moving too fast, like hydrophobic interactions or van der Waals. - When Protein gets hydrolyzed you lose peptide bonds and therefore it can never be renatured because you are breaking down the monomers of protein. Even if you put it into optimal conditions it would not be removed. - A protein can only be renatured if it is not intensely damaged and is placed back into its optimal conditions. Example: Applying urea (highly polar) to a protein can affect hydrogen bonding and disrupt protein structure and then remove urea and place the protein where there's an absence of urea it can renature. So you must place it back into an optimal condition?

Similarities / Differences between Proteins and Nucleic Acids

Proteins can be found on the cell membrane while nucleic acids do not appear on the membrane. Both have monomers that have "backbones." Amino acids have backbones that consist of an alpha carbon that is bonded to an amino group, carboxyl group and a hydrogen. Polypeptides are also synthesized in different levels and are from the N-terminus(the beginning) to the C-terminus (the end). Nucleic acids have backbones that consist of a phosphate group and a five carbon sugar. Both have monomers that have a region that confers their diversity. The R groups of amino acids vary and the nitrogenous bases of nucleotides vary. Also, they're both macromolecules.

Similarities / Differences between DNA vs RNA

RNA is usually single stranded while DNA is usually double stranded. DNA has thymine while RNA has uracil. RNA is made up of the ribose sugar which has a hydroxyl (OH) group at the 2' carbon while DNA is made up of deoxyribose sugar which has a hydrogen (H) at the 2' carbon (deoxy = missing an oxygen). Both DNA and RNA exhibit phosphodiester bonds between the backbones of their monomers. Both DNA and RNA monomers have a phosphate group, pentose (five carbon sugar) and nitrogenous bases (Adenine, Cytosine, Guanine). Because of their phosphate group they are both negatively charged.

Similarities / Differences between Saturated and Unsaturated Fats

Saturated Fats = carbon molecules are full with single bonds; no double bonds; solid at room temperature. (Rigid, less fluid) - Closer proximity, more hydrophobic interactions (remember that hydrophobic interactions occur between nonpolar molecules in a polar solvent, such as water), less fluid - Ex. butter, coconut oil Unsaturated Fats = contains double bonds & it is generally liquid at room temperature (cannot stack) (More fluid due to the kink) - Ex. vegetable oil

Monomers of the macromolecules

Simple Sugars - Polysaccharides Fatty Acids - Fats, Lipids, Membranes - Lipids are not Macromolecules. Amino Acids - Proteins Nucleotides - Nucleic Acids.

Roles of Sugar

Simple Sugars are the monomers of Complex Sugars. Simple sugars are known as monosaccharides which give for information. They function in Energy storage, structure(structural integrity), and skeletal rearrangements (Change of carbon-based structure to facilitate reactions)

Types of polysaccharides What kind of monomers creates its polymers? What kind of covalent glycosidic bonds create these polymers? Where do we see these polymers? What are their functions? What is able to facilitate hydrolysis when it comes to humans digesting Potato(starch) vs corn(cellulose)?

Starch, Glycogen, Cellulose - Starch has less branching and stores energy can be broken to tap into the energy. Cellulose has structure and imparts integrity on plants and this can be seen with the close-packed linear polysaccharides not accessible. - Amylase can access linkage in starch but cannot do that for cellulose because of the different types of monomers being bridged together a-glucose vs. b-glucose.

Distinctions in Macromolecules

Sugars, Nucleic Acids, Proteins, and Lipids are large biological molecules but only the first 3 are macromolecules and not lipids because they cannot polymerize and continue to create long chains like the other ones.

Protein Tethering

Tethering used to keep proteins in place. Either tethered to extracellular matrix or cytoskeleton.

Nucleotides : Polymerization

The 3' connects to the phosphate group a the 5' carbon of another nucleotide. The phosphate rotates upward. This occurs through dehydration synthesis forming phosphodiester linkages which are a form of covalent bonding. - Links in a 5' to 3' fashion

Tonicity

The ability of a solution surrounding a cell to cause that cell to gain or lose water.

Nucleotides (Monomer for Nucleic Acids)

The building blocks of nucleic acids; they consist of a five-carbon sugar(pentose), a phosphate, and a nitrogenous base. These are the repositories for genetic information. A nucleoside is the same thing but no phosphate.

Unsaturated Fatty Acids If I have Unsaturated Fatty Acids compared to Saturated Fatty acids do I have more or less hydrophobic and van der Waals interactions?

The carboxyl group here has donated proton to the environment putting it in an ionized state. - Unsaturated fatty acids have at least one kink caused by a double bond which means it's not saturated completely with hydrogens. These unsaturated fatty acids create a lot of space with that kink which reduces the number of noncovalent bonds as opposed to saturated fatty acids because we are inhibiting close proximity bonding. - Two kinds of unsaturated. Cis and Trans. Cis is hydrogens on the same side (maximizing space) creating kink whereas Trans is on opposing sides which do not have to maximize space and therefore present with no kink and behave like saturated fatty acid.

Saturated Fatty Acids

The carboxyl group here has donated proton to the environment putting it in an ionized state. Saturated fatty acids have maximized the number of hydrogens and no double bonds are present. This allows hydrocarbon tails to stack next to each other and it can get into close proximity. The close proximity between these hydrophobic tails is coming close to one another and generate noncovalent bonds. This allows high amounts of fatty acids to stabilize and reduce movement causing it to solidify at room temperature. Presence of van der Waals and hydrophobic interactions. This means they can dissociate readily with little energy. Takes up less space then Unsaturated Fatty Acids.

Building Proteins // Linking Amino Acids

The covalent bond between the amino group of one amino acid and the carboxyl group of another amino acid. - This creates polypeptides - Ranges in length - Proteins have a unique linear sequence that can be SIMILAR but no the same. - This linear structure formed through peptide bonds create the primary structure of the protein - Creates an Amino end (N terminus) (available) and Carboxyl End (C terminus) Direction of polymerization. Starts with N terminus to C terminus (available for peptide bond with incoming amino acids.)

Quaternary structure Do all proteins reach Quaternary structure? Can a single polypeptide exist on it own? if so which stage would this be in?

The fourth level of protein structure; the shape resulting from the association of two or more polypeptide subunits. - 2 or more polypeptides that are called subunits. - hemoglobin has 4 subunits = 4 polypeptides. - Quaternary structure is different from protein-protein interactions. - The example she gave was with Hemoglobin which is a quarternary structure that interacts with another protein. this interaction is not quarternary but only protein-protein interaction. - Proteins that behave normally should be at the tertiary level. If they have multiple sub-units they can reach Quarternary. - Globular, multiple polypeptides interacting in various types of interactions. - Bonds in tertiary also occur in Quaternary.

Nucleotides : Phosphate Group

The phosphate groups in Nucleotides give it a negative charge. Achieved through covalent bonding. It can range from 1 to 3 Phosphate group. 3 means its full of energy but 1 means little energy.

What mechanism allows us to separate subunits?

Through a hydrolysis reaction. Use of covalent bonding indicated by solid lines. A - B. This is not achieved by simply putting them next to each other but rather are driven by other things. Just having water won't work. Using enzymes to facilitate is one way.

DNA - RNA What is transcription? What is translation? Does RNA stay or leave the nucleus? How do we have available DNA and RNA? How are we able to polymerize our protein Structure?

Transcription - DNA to RNA Translation - RNA to Protein (Outside of cell into the cytoplasm) Protein Synthesis initially starts into the cytoplasm.

Building Sugars

Use of dehydration synthesis to form Glycosidic bonds (covalent) between hydroxyl functional groups. In this image, it is a disaccharide not poly yet. An oligosaccharide is 3 monosaccharides but any more would be poly. - The presence of hydroxyl groups lends polarity. There are ode hydroxyl groups indicating net polarity.

Osmosis

Water will move into higher concentration of solute.

DNA where are my covalent bonds? where are my non-covalent bonds?

When we build one polynucleotide which will be one single strand of DNA it will be only covalent bonds. However when you insert that second polynucleotide to form a double helix structure then you have non-covalent bonds specifically Hydrogen bonds forming between the Nitrogenous bases. These strands run anti-parallel. It requires a lot of energy and high temperature to dissociate. Very stable polynucleotide.

Hydrophobic interactions

a type of weak chemical interaction caused when molecules that do not mix with water coalesce to exclude water.

Isotonic Solutions (Animal cells love this) makes plants flacid.

solutions separated by a membrane and containing an equal concentration of non-permeating solutes