functions and types
Long-term energy storage and structure
Cell membrane structure
Cell signaling
•Main types:
•Fats
•Phospholipids
•Steroids
function monomers and polymers
•Function:
•Store and transmit hereditary information
•Monomer – Nucleotide
•Polymer – Deoxyribose Nucleic Acid (DNA) & Ribose Nucleic Acid (RNA)
•Genetic info flows from DNA à RNA à protein
side and major functions
•Functions:
•Structural support
•Storage
•Transport of other substances
•Signaling from one part of the organism to the other
•Movement
•Defense against foreign substances
•Enzymes!!! (speed up chemical rxns)
enzymes most important
what are steroids
•Steroids are Lipids characterized by a carbon skeleton, consisting of 4 interconnected rings
•Hydrophobic/insoluble in water (why they are considered lipids)
•Used in cell membranes and signaling molecules (hormones)
how are hydrogen and hydroxide ions formed and what are they
uH20 molecules break apart & form ions (charged)
uWater à hydroxide ion (OH-) + hydrogen ion (H+)
polar or nonpolar
mainly nonpolar (hydrophobic)
what is dna structure what is it made of
•DNA is made up of repeating molecules called NUCLEOTIDES
•Each nucleotide contains:
- Phosphate Group
- 5-Carbon sugar (deoxyribose)
- Nitrogenous base
monomers and polymers
•Amino acid consists of an amino group, carboxyl group and R group
•R groups determine the property of the amino acid and therefore the folding (shape)
•Different R groups can cause proteins to be polar, nonpolar, ionic, or even have acid/base properties
•Polymer- Polypeptide
Monomers: Proteins are made of 20 different monomer amino acids joined by peptide bonds (also called “polypeptides”)
•Peptide bonds are covalent bonds between amino acids
•Created through dehydration synthesis
The folding of one or more polypeptides forms a protein
what is denaturation and what causes it
•The unfolding of a protein, modifying its shape and, therefore its function.
•Results in the loss of the protein's activity, rendering it inactive
•Enzyme function under optimal conditions (temperature, pH, salinity, etc.)
•Changes in those conditions can cause denaturation.
how does the ph scale measure
uShows concentration of H+ ions in solution.
uRanges from 0 to 14.
uAt pH 7, the concentration of H+ ions & OH- ions are equal
monomers and polymers
•Monomer- fatty acid
•Fatty acid
•A long carbon skeleton with carboxyl group head and a hydrocarbon tail
•Two types: Saturated and unsaturated
•Polymer- Triglyceride
•Triglyceride
•Three fatty acids linked to one glycerol molecule
what are the nucleotides that make up dna and what are their groups
•Pyrimidine
•6 membered ring made of carbon and nitrogen atoms
•Cytosine (C) and Thymine (T)
•Purine
•6 membered ring fused to a five membered ring
•Two ring structure
•Adenine(A) and Guanine Two-ring (G)
•Phosphodiester
•Covalent bonds holding nucleotides together
structurs/conformations of the peptides in proteins
1.Primary Structure – a sequence of amino acids, connected by peptide bonds.
•Secondary Structure– Hydrogen bonding occurs between amino and carbonyl groups of amino acids. Causes spiraling or folding of the polypeptide.
•Alpha helix (spiral)
•Beta-pleated sheet (folded/flat wavy sheets)
on the ph scale what is acidic basic and nuetral
uH+ = OH-
uDescribed as neutral
uPure H2O
uSolutions w/ a pH less than 7 are acidic
uSolutions w/ a pH greater than 7 are basic, or alkaline
what are fatty acids and what is saturated and unsaturated
Fatty acid
•A long carbon skeleton with carboxyl group head and a hydrocarbon tail
A long carbon skeleton with carboxyl group head and a hydrocarbon tail
•Two types: Saturated and unsaturated
Saturated Fatty Acids have no double bonds between carbon atoms. contain a maximum number of hydrogen atoms, usually found in animals, and solidify at room temperature-heart attack
•Unsaturated Fatty Acids have one or more double and/or triple bonds between carbon atoms and are liquids at room temperature, easier to breakdown due to kinked shape-no no heart attack
dna structure and what bonds with what
•Double helix
•Two chains of nucleotides that spiral
•Hydrogen bonds
•Hold two chains of nucleotides together
•H-bonds are summative – strength in numbers
•
•Purines and pyrimidines bind together with hydrogen bonds
•Adenine ----Thymine (2 H-bonds)
Cytosine ---- Guanine (3 H-bonds)
more structures of peptides
3.Tertiary Structure - Irregular contortions from bonding between R groups of various
•Different R groups give different shapes (shape/structure = function)
what does ph regulation show
homeostasis/buffer system
what is a triglyceride and how do they relate to phosphate groups
•Three fatty acids linked to one glycerol molecule
•Phospholipids are lipid but a variation of a triglyceride, one fatty acid chain is replaced by a phosphate group. 1 glycerol, 2 fatty acids, and 1 phosphate group.
•The head is hydrophilic and contains the glycerol and phosphate group.
•The tail is hydrophobic and contains two fatty acids, one is unsaturated and the other is saturated.
contrasts between dna and rna
•DNA
•Deoxyribonucleic acid
•Deoxyribose sugar
•Bases:
Adenine
Guanine
Cytosine
Thymine
Double-stranded normally
•RNA
•Ribonucleic acid
•Ribose sugar
•Bases:
Adenine
Guanine
Cytosine
Uracil
•Single-stranded
how do enzymes speed up this conformation
•Enzymatic proteins facilitate/speed up chemical rxns (end in –ase)
•Chemical reactions require energy to start. Activation energy is the energy needed to start chemical rxns
•Enzymes lower the activation energy