Synthesis of Polymers (Dehydration Reaction)

-H and -OH are removed (~water) 

-> Subunits join into a polymer

i.e. components are dehydrated

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Polymer is split into smaller subunits by adding -H and

-OH (~water)

i.e. polymer is hydrolyzed

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Monosaccharides can rotate between linear and ring form Beta Glucose hase OH pointing up and O on the bottom Alpha Glucose has OH pointing down and O on top

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Important monosaccharide

6 carbon molecule = hexose Main energy source for cells Monomer unit of important polysaccharides

Important monosaccharide

5 Carbon Molecules

Difference based on 2' hydroxyl for Ribose and 2' hydrogen for 2-Deoxyribose

Components of nucleotides

Important Plant Polysaccharide

Short term energy storage

Polymer of alpha (1->4) glucose

Digestable in animals using amylase which is an enzy that digest starch by hydrolyzing alpha linkage

Important Animal Polysaccharide

Short term energy storage

Polymer of alpha (1->4) glucose

Structural Component (i.e. plant cell walls)

Polymer of beta (1->4) glucose

Not digestable in animals (requires cellulase)

Alpha linkage polysaccharides can be digested by amylase an enzyme found in animals

Beta linkage can not be digested by animals, requires cellulase. Beta linkage alternates position of OH and H

Important polysaccharide

Structural component

Polymer of modified glucose monomer

 Not true polymer (no monomer subunit)

Diverse group

Hydrophobic

Water insoluble 

Fat soluble

Fatty Acids: components of other lipids

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Triglycerides: long term energy source 

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Steriods: Signaling molecules and membrane components

Main component of cell membrane

Organelle and plasma membrane made up of lipid bilayer

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Structure:

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20 different amino acids

Classified based on R group

How to recognize: Have CH, C, or H at the end of R chain

Glycine (Gly)

Alanine (Ala)

Valine (Val)

Leucine (Leu)

Isoleucine (Ile)

Methionine (Met)

Phenylalanine (Phe)

Tryptophan (Trp)

Proline (Pro)

How to recognize: Have an OH, O, or SH at the end of R chain

Serine(Ser)

Threonine(Thr)

Cyestine(Cys)

Tyrosine(Tyr)

Asparagine(Asn)

Glutamine(Gln)

How to recognize: R chain ends in O or NH

Aspartate (Asp)

Glutamate (Glu)

Lysine (Lys)

Argininge (Arg)

Histidine (His)

Aspartate (Asp)

Glutamate (Glu)

Mnemonic: Acid is a drug. Asparine is a drug and glue can be a drug if you huff it 

How to recognized: The rest of the Polar Charged Amino Acids

Lysine (Lys)

Arginine (Arg)

Histidine (His)

Molecule with multiple peptide bonds.

A bond between 2 Amino Acids via dehydration synthesis.

N-terminal end is the H

C-terminal end is the OH

Mnemonic: Remember because if you think N terminal is OH put them together and it makes NOH

Amino acids join together to form polypeptide chain

Influences formation of all subsequent levels

Specified by a corresponding gene sequence in the DNA

Polypeptide chain is coiled and folded on itself

Does not involve R groups

Stabilized by H-bonds

Alpha Helix = Coiled

Beta Pleated Sheet = Folded (paperfan)

Levels of Protein Structure: Tertiary (3) Structure

Creates 3D shape of protein 

Layered over the  patterns of secondary structure

Result of interactions between either R groups are interacting with other R groups or they are interacting peptide backbone (amino acid without R group)

Disulfide Bond or Bridge: When SUlfurs in R group bond together (Cyestine)

Ionic Bond or Salt Bride

Hydrophobic Interactions or Pockets: Minimizes nonpolar hydrophobic molecules from interacting with water

Van der Waals Interactions or London Dispersion Forces

Found only in proteins composed of tow ore more polypeptide chains each with its own 1, 2 and 3 structure

A carboxyl group is the -COOH that is usually attached to a carbon chain (R group) to make a whole molecule which is called a carboxylic acid.

For example: HCOOH by itself is carboxylic acid which is in bee venom.

Proteins that comprise Hemoglobin, bond incorrectly which creates a faulty shaped Hemoglobin that causes blood cells to clump and cluster blocking the flow of blood

Information molecules

Polymers of nucleotides

DNA= Doxyribonucleic Acid

 - Hereditary Information

RNA = Ribonucleic Acid

 - Transfers information from DNA to protein

 - Some ribozymes (catalytic RNA)

 - Some viral genomes

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One carbon ring

Uracil (RNA)

Thymine (DNA)

Cytosine

Two fused carbon rings

Adenine 

Guanine

Ag is silver which is a pure substance.

Nucleotide Monomer

Pentose Sugar (ribose if OH or deoxyribose if H) + Nitrogenous Base

Phosphate group is always attached to 5'

5' end ends in phosphate, 3' end does not

Bond between nucleoties around phosphate group in polynucleotide

Base pairs joined by hydrogen bonding

Adenine (A) -> Thymine (T)

Guanine (G) -> Cytosine (C)

For RNA replace T with U

1958

Suppourts semiconservative model

Enzyme that catalyzes the polymerization of dNTPs into a DNA strand

Cannot synthesize polynucleotides by itself, it needs a pre-existing chain

Can only add dNTPs to 3' OH

DNA synthesis occurs only in the 5'->3' direction

• 3'->5'
• Replication occurs in same direction as Replication Fork

• 5'->3'
• Replication occurs in opposite direction from Replication Fork
• Replication occurs Discontinously in fragments (Okazaki fragments)

• Location(s) on chromosome(s) where DNA is opened up for replication
• Each Ori forms a pair of replication forks
• Move in opposite directions from common Ori
• Replication cuntinues until forks collide
• bacteria have one per chromosome; Eukaryotic chromosomes have many

Alleviates stress caused by unwinding of DNA

Stabalize unwound DNA strands

Unwinds and seperates DNA strands

Fills in gaps between Okazaki fragments

Synthesizes RNA primers using DNA strand as template

• Short repeating sequences of non-coding DNA
• Prolong life of the chromosome

• Reverse transciptase: can synthesize DNA from an RNA template
• Carries its own RNA primer
• Elongates telomeres after DNA replication
• Found in germ cells other highly active cells (e.g. stem cells)