Macromolecules Lect. 4 Flashcards
Salts
Any ionic compound that does not contain H+ cation or OH anion. produced from the reaction between a acid and base. Cation base and anion acid
Carbohydrates
starches, sugars: organic molecules that always have a carbon, hydrogen, oxygen, polar
Monosacchrides
simple building sugar blocks , contain C, H, O and simplest form of carbohydrates
Deoxyribose (DNA) and ribose (RNA) are types of these
The joining of two monosacchrides caused by dehydration sythesis.
Isomerism
chemical compound with the same formual but different structure.
Disaccharide
Two joined monosaccharide’s formed through dehydration synthesis.
Glycosidic Bonds
Between indepedent glucose bonds
Polysaccharides
long chains of monosaccharides:
1. Starches (Alpha) easily digested and have alpha glycosidic linkages. Increase gut motility, insoluble fibers. Enzymes are better at breaking these.
2. Cellulose (fiber) hard to digest (soluble fiber)
3. Glycogen (easy to digest) stored in liver, muscle and has beta glycosidic linkages made. Stored form of glucose. Ennzymes cannot break.
Hyperglyecemia
High blood glucose/sugar, if insluin cannot prepare cells for glucose
Type 1 Insulin Dependent Diabetes Mellitus
Destroys Beta cells so there is no insluin
Type 2: Non insulin dependent
Cell resistance ; hyperseceretion of Insulin led to cells stop taking in glucose.
Lipids
Nonplar, insoluble, and hyrophobic
must have a transport mechanisum as they cannot dissolve.
6 groups:
fatty acids, eiconsanoid, glycerides, steriods, phospolipids, glycolipids
Fatty Acids
Long hydrocarbons with carboxylic acid group at one end which is hydrophillic. Mainly nonpolar: Allow them to attach to building blocks. Only the hydrophillic end likes water so longer tails are less souble. Building blocks of fats
Saturated vs Unsaturated vs trans fats
Saturated are each carbon atom is attached, no double bonds only single
Unsaturated there is at least 1 double bond
Transfats have hydrogen on opposite sides and a trans double bond
econsanoids
non-polar, lipids which are derived from arachidonic acid (cannot be sythesized) two types:
Leukotrienes: white blood cells released with prostaglandins, inflammatory response
Prostaglandin: local hormone and causes regional inflammation due to damage
Glycerides
A result of dehydration synthesis between glycerol and fatty acids chains. One of three dehydration sythesis reactions result in systhesis of triglycerides.
Triglycerides
The largest (fat) energy stored in the body and have three main functions. Contains a glycerol and 3 fatty acid chains and made from 2 dehydration reactions.
- energy source
-insulation
-Protection
Type of glycerides
Fats (ketosis)
(glucose replacement) Result from excess breakdown of fats which create ketones in the liver if no glycogen is available. Leads to ketoacidosis High amounts of hydronium.
Steriods
Large lipid molecules based on 4 hydrocarbon structure. (nonpolar) Cholestrol is a buidling block for other steriods in the body.
Steroid function
- Plasma membrane (cholesterol structure)
- Sex hormones (testostrone, estrogen)
- Tissue metabolism and mineral balance (aldoestrone na regulation. Cortisol: reduces inflam, stress, moblize glucose, and boost immune, mainatin blood sugar)
- Bile salt ( cholestral helps to emulsify fats breakdown
Coritsol
- maintains blood pressure
- Bolster immunity
- reduces inflammation
Phosplopidid
Sythesized by body from fatty acids. Phosphate group links to a diglyceride to a non-lipid. Make up the cell’s membrane
Has a polar (hydrophillic head) and a non polar (hydrohobic tail)
ECF (mainly h20)
Glycolipids
similar to carbohydrate and replaces phosphate
Proteins
The most abundant by weight macromocule in the body. Contains C,H,O,N and is resposnible for:
- Support (creates the framework for the body)
- Movement( muscle contraction , actin and myosin)
- Transport (hemogloboin, ,move insoluble moluecles)
- Buffering ( prevent dangerous pH changes
- Coordination Control (protein hormones influence metabolic functions) help regulate enzymes
- Defence ( skin protection)
Amino groups
Soluble contains amino group, R group ( makes special) , and a carboxylic Acid (COOH)
Dehydration Sythesis and Hydroplysis
Dehydration is the removal of water which creates bonds and froms new molecules while hydrolysis is adding water and the bonds link amino acids are broken by this water
Structures of Proteins
Primary
Secondary
Teritary
Quatenary
Primary to Secondary
Amino acid sequence is a polypeptide that forms a secodonary structure. The primary chain forms alpha helixes and beta sheets (sprials) due to the weakened interactions between amino groups of hydrogens.
Tertiary to Quantenary
When the interactions between polypetide chains surround water, it will begin to coil and fold up. The proteins 3D shape takes place due to the cystine which binds itself forming cross linkages as well as the R-group interactions. These coils are premanent.
Protein Issues
Sickle Cell Amenia: 1 amino group affected
Misfolded Protein (jackob diease)
Primary Structure: valine is replaced by guanine a less soluble one
Fibrous and Globular Proteins
Fibrous form extended sheets of strands that are tough, insoluble
Globular proteins are compact, soluble proteins , such as enzymes , hormones and they move quickly
Enzyme
Proteins that catalyze reactions by weakening bonds which lowers the activation energy of a reaction. They have an active site which have substrates that bind to them.
Characteristics of Enzymes
Specific: each enzyme catalyst one reaction type
Saturation limits: rate of enzyme reaction is directly proportional to substrates and enzymes
Regulation: cell contains enzymes that can be turned on and off , change shape
Denatured enzymes are caused by ph change and temperature
Enzymes
Enzymes are a protein that catalyizes reactions by weakening bonds which lowers the activation energy of the reaction. The reactants are the substrates in these reactions which bind to the active site. Bond is formed storing the energy and water is released, the product is created and the substrate is released.
Characteristics of Enzymes
Specific: each enzyme catalyzes one reaction type
Saturation limit: the rate of enzyme reaction is directly proportional to the substrate and enzyme
Regulation: each cell contain enzymes that can be turned on and off by a change in shape
Denaturation of an enzyme is caused by the pH and temperature
Cofactors/ Coenzymes
Cofactors (change sturcture) are ions that are not proteins, organic and bind before substrate. Co enzymes are non protein molecules, that are organic.
Glycoproteins and Proteoglycans
Glycoproteins are large protein that have a small carbohydrate group
Proteoglycans are a large polysaccharide linked with polypeptide bonds. Subclass of glycoproteins; the carbohydrate group contains polysaccahride amino groups
Nucleic Acid
The largest organic molecule , two types are DNA and RNA
DNA / RNA
Deoxyribose nucleic acids determine the inherited characteristics, body structure, protein synthesis, cellular metabolism
Contain a phosphate backbone
DNA has a deoxyribose sugar
RNA carries out the DNA, makes proteins and carries out protein synthesis. Has a ribose sugar
Nucleotide Structure
Phosphate group attached to a pentose and nitrogenous bases
Phosphate ladder
Dehydration Syethesis connects the pentose of a nucleotide with the phosphate of another.
nitrogenous pairs
Known as complementary paring;
DNA: Adenine –> thymine
Cytosine–> Guanine
RNA: Adenine–> Uracil
Connected via weak hydrogen bonding
Pyramides: Cytosine, Thymine, Uracil
Pyrites: Adenine and Guanine LARGER
Differences between DNA/RNA
- DNA is double helix structure and RNA is single stranded
- DNA contains thymine, RNA contains Uracil
- DNA coodirnates most of the functions while RNA follows and carries instructions out
- DNA is in the nucleus, RNA in the cytoplasm
- DNA contains deoxyribose, RNA has ribose sugar
Phosphate Bonding
Created through phosphorylation, one phosphate is added to ADP which stores the energy in its bonds. This is key to ATP making energy.
ADP + phosphate+ energy –> ATP and water
Bonds are unstable
