Lecture 2: Biomolecules Flashcards
What are biomolecules?
Biomolecules are an organic molecule that is commonly associated with life
Define organic molecule
contains carbon
What is the general
Formula of Carbohydrates?
C(n) H(2n) O(n)
Are most carbohydrates Hydrophilic or Hydrophobic
Hydrophilic
What are carbohydrates typically used for?
Structure and energy
Define Monosaccharides and give 2 examples
Are a simple sugar, five carbons or six carbon
ex; Ribose, Glucose
Define Disaccharides
Consist of Glucose and another monosaccharide
Define Polysaccharide
Give 2 examples
Are glucose polymers, all living cells store glucose for energy in this form
Ex; Cellulose and Starch
Nucleotides and Nucleic Acids are involved in what
energy metabolism and signaling
A nucleotide consists of what three things
1) One or more phosphate groups
2) A 5-carbon sugar
3) A ring structure called a nitrogenous base
The structure of a nitrogenous base determines whether the nucleotide is
Adenosine, Cytosine, Guanosine, or Thymidine
Define ATP
Is Adenosine Triphosphate which is the basic molecule of energy storage in most mammals and organisms
Adenosine is a
Neurotransmitter
Define GTP
Is Guanosine Triphosphate which is an energy source in physiological chemical reactions
Define cAMP
What enzyme converts ATP to cAMP
An important signaling molecule within cell
Adenyly cyclase
Define cGMP
What enzyme converts GTP to cGMP
An important signaling molecule within the cell
Guanylyl cyclase
Lipids contain
Mostly carbon, hydrogen, few oxygen, nitrogen and phosphorus
Are lipids typically hydrophilic or hydrophobic molecules
Hydrophobic or have hydrophobic parts
What are the 5 groups of Lipids?
1) Fatty acids
2) Glycerides
3) Phospholipids and Sphingolipids
4) Steroids
5) Eicosanoids
Fatty acid properties are
a long chain with 8-28 carbon atoms bound to hydrogen with a carbonyl functional group
Saturated fatty acide have ____ bonds and a ____ chain and are ____ at room temp
no double bonds , straight solid
Unsaturated fatty acids have ______ bonds and a _____ chain and are ____ at room temp
double bonds, kinked, liquid
What are the 3 roles of lipids
1) Structure of cell
2) Energy source
3) Communication both within and between cells
Glycerides are a derivative or what
derivative of Fatty acids
Glycerides typically do what to water
takes it out
What are the three kinds of glycerides
Mono-
Diglyceride
Tri-
Phospholipids and Sphingolipids contain
a phosphate group, a diglyceride and an R group
Phospholipids are _____ molecules that have _____ head and _____ tails
Amphipathic molecules with polar heads and non-polar tails
Define amphipathic
having both hydrophilic and hydrophobic molecules
Phospholipids come in 3 shapes what are they
Bilayer,
Micelles (droplets)
Liposomes (3D, aqueous center)
Phospholipids are converted to Sphingolipids by
removing the glycerol and changing it into sphingosine
Phospholipids are _____ than sphingolipids
smaller
What is the basic structure of Steroids?
Consists three six-carbon ring with one five carbon ring (17 carbon)
Different function group (R group)
What two areas do steroids play a role in
communication and cell structure
What are 2 examples of steroids
Testosterone and cortisol
Eicosanoids consist of ____ carbons and derived from
20, fatty acid arachidonic acid
Eicosanoids play a role in
communication within cells
Proteins are ________ with _____ chains made up of _____
macromolecules , linear and amino acids
How many amino acids are encoded by the universal genetic code; and of them how many are essential (need to be consumed)
20 and 9
Amino acids can be
acidic, basic, polar, non-polar
A short chain of amino acids are called _____ where as a long chain are called ____
Peptides; Proteins
What are the four structures of Proteins
Primary
secondary
tertiary
quaternary
Define primary structures of proteins
Linear sequence, 10-100 AA
Define secondary structures of proteins
Covalent bond angles between amino acids. Can be a-helix or B-pleated sheets
Define Tertiary proteins
A 3D shape , looks like random lines?
Define quaternary structures of proteins
Muletiple subunits combined with noncovalent bonds
Can be fibrous or globular
Give an example of a fibrous protein and a globular protein
collagen = fibrous hemoglobin = globular
Proteins are the ____________ ___________ of cells
Molecular tools
What are the 7 functional groups of proteins?
1) Enzymes
2) Membrane transporters
3) Signal molecules
4) Receptors
5) Binding proteins
6) Regulatory proteins
7) Immunoglobulins
Enzymes are
biological catalysts, speed up chemical reactions
Membrane transporters
May form channel in cell membrane or bind to molecule and carry it through a membrane
Signal molecules
signal other molecules
Receptors are proteins that
bind signal molecules and initiate cellular response
Binding proteins are found and do what
give an ex
are mostly found in the ECF , bind and transport molecules throughout the body
ex; hemoglobin
Immunoglobulins are also called what and do what
antibodies and help protect the body from foreign substances
Define a Ligand
a molecule that binds to a protein binding site
Define an Agonist ligand
A ligand that binds to a protein binding site and alters the state of said protein, resulting in a biological response
Define Antagonist ligands and give the two types
A Ligand that reduces the action of an agonist, binds but causes no biological response
can be competitive (act to block the agonist at its binding site) or Allosteric (act to block the agonist by binding to the protein away from the binding site and inactive the binding site)
What is another name for n antagonist ligand
Inhibitor
Define affinity
A protein binds a ligand with affinity
high = strong
Rate of protein binding can be modified by what 3 things
1) Depends on type of protein
2) ligand concentration
3) Saturation
Define binding regulatory subunits
They change protein’s activity to bind a ligand, or change the proteins activity/ability to create a response
Define Isoforms
Closely related proteins whose function is similar but whose affinity for ligands differ
What can pH or temperature cause
Structural changes
True or False; Phosphorylation does not mean it activates the protein?
True
Describe phosphorylation
Adding a phosphor via the enzyme kinase
Describe Dephosphorylating
Removing a phosphor via the enzyme phosphatases
When a Phosphors is removed from ATP it turns into what and energy us _____
ADP and energy is released
What is the difference between an organic molecule and a biomolecule?
Organic molecule is a molecule that contains carbon, biomolecules is an organic molecule that is commonly associated with life , ex carbohydrates, lipids
Why would a cell store glucose as glycogen?
Because polysaccharides are glucose polymers and all living cells store glucose for energy in this form
Structurally, what is different between a phospholipid and a sphingolipid
sphingolipid have a sphingosine backbone and tail with no glycerol
Why are some fatty acids considered saturated and some considered unsaturated?
Saturated fatty acids = double bonds, solid at room temp
Unsaturated fatty acids = no double bonds, liquid at room temp
What is the significance of different R-Groups
R groups alter amino acids
True or False; All amino acids are considered acidic
False
What does adding an antagonist do to reaction velocity?
Slows down the reaction because antagonist binds to a protein and decreases its activity
What role do cofactors play in activation?
attaches to their protein before the binding site will become active and bind to ligand
Describe chemical modulators
Molecules that bind covalently or non covalently to a protein and alter their binding ability or their activity
Describe irreversible antagonists
compete with the customary ligand for binding sites
Allosteric modulators
bind reversibility to protein at regulatory site away from the binding site, by changing the shape at the binding site
Define and distinguish between the processes of up-regulation and down- regulation
Down-Regulation = removal of proteins Up-Regulation = production of new proteins
Define saturation and describe how proteins can reach the point of saturation
saturation is when concentration of ligand exceed some point, protein molecules have no free binding site and rate reaches a max rate
