powerpoint 22 Aug
Download
Report
Transcript powerpoint 22 Aug
What can you tell me about this compound?
pyridoxine
CH2OH
HO
OH
N
H+
What can you tell me about this compound?
P
O
O
OH
OH
OH
IP3
O
P
P
What can you tell me about this compound?
H3C
NH
H2C
OH
CH
epinephrine
OH
OH
What can you tell me about this compound?
beta-carotene
Chapter 2
Apply Problem #5
If an aqueous (water) extract does not work but one
using benzene as the solvent does have an effect, what
might you conclude about the chemical nature of the
hormone? explain.
Hormone is lipophilic or nonpolar.
Explain:
Hormone dissolves in benzene, an organic solvent (nonpolar)
but doesn’t dissolve in polar solvent (water).
Proteins
The other main component of the cell membrane.
Functions of Protein
Transport
channels
pumps
carriers
Communication
receptors
signaling molecules
hormones
“flags”
Enzymes
Structure
Collagen, keratin, bone matrix, intracellular microtubules
Antibodies
Movement
Muscle cells are 20% actin (protein)
Amino Acid Structure
O
O
+
H3N
H2N
CH
CH
OH
R
R group can be
• polar or nonpolar
• big or small
• charged – acidic or basic
R
O-
Amino acids – R groups
lysine
O
O
H2N
CH
CH2
CH2
CH2
CH2
NH2
C
OH
H2N
CH
C
OH
CH2
cysteine
SH
Amino acids – R groups
O
H2N
CH
CH2
C
aspartic acid
O
OH
tryptophan
H2N
CH
C
CH2
C
HN
OH
O
OH
Amino acids
O
H3C
H2N
CH
C
OH
CH2
NH
H2C
OH
CH
epinephrine
OH
tryosine
OH
OH
Peptides – dipetide formation
Formation from amino
acids: FOX fig 2.25
O
O
H2N
cysteine
CH
C
H2N
OH
CH
C
OH
H
CH2
glycine
SH
O
H2N
dipeptide
CH
CH2
SH
C
NH2
CH
H
COOH
+
H 2O
Tripeptide - glutathione
• glycine
• cysteine
• glutamic acid
Peptides
O
O
H2N
CH
C
OH
+
H2N
CH
CH2
CH2
CH2
SH
C
C
NH2
CH
COOH
H
dipeptide
O
OH
glutamic acid
OH
O
O
C
CH
H2
C
H2
C
C
NH2
O
H2N
CH
CH2
glutathione
SH
C
NH2
CH
H
COOH
Protein
Four levels of structural organization
Primary structure
Amino acid sequence
gly-cys-ala-trp-glu-asp-gly-tyr-cys-ala Secondary structure
Sections of peptide chain coil or fold into either:
Alpha helix
Beta sheet
Tertiary structure
Whole peptide chain (protein) folds/coils around itself
H bonding, sulfide bridges, non-polar/non-polar interactions
Quaternary structure
More than one peptide chain associated with each other
Proteins
(FOX fig 2.26)
Tertiary Structure (FOX fig 2.27)
Protein Synthesis
within the context of homeostasis.
Objectives
Review
how proteins are synthesized
Give an example of an effector action
Review key organelles
Preview regulation of ions
Preview endocrine signaling
Protein Synthesis
within the context of homeostasis.
Negative Feedback:
Sensor
detects a change parameter’s level
Control unit activates an effector
Effect is to return parameter to normal level
Typical effector action is to make a protein
Another effect is to activate a protein
protein
activation can lead to the release of
hormone or neurotransmitter
protein activated is often an enzyme
Protein Synthesis Example:
Aldosterone
What is aldosterone?
Steroid
hormone produced by adrenal cortex
It is a mineralocorticoid
Promotes the retention of Na+ and loss of K+
What induces the release of aldosterone?
Low
Na+ and high K+
Target organ?
Kidney
– epithelial cells of distal tubule
carrier protein (albumin)
aldosterone
target cell
plasma membrane
Aldosterone on carrier approaches the
cell membrane
Aldosterone diffuses readily into the
lipophilic membrane.
Aldosterone receptor picks up
aldosterone and moves it into the cell.
aldosterone receptor
Aldosterone receptor complex heads
towards the nucleus.
know
cell
structures
Translation
(FOX fig 3.24)
Microtubules aid
movement of vesicles
to cell membrane
Pumps/channels
are degraded in
lysosomes when
no longer needed
Carbohydrates
Contain CH2O
6 carbon sugars – C6H12O6
glucose (glu)
fructose (fru)
galactose (gal)
5 carbon sugars – C5H10O5
ribose
DNA
RNA
Carbohydrates
If glucose and galactose have the same formula
(C6H12O6) what is the difference?
structural isomers (FOX fig 2.13)
CHO
CH2OH
H
O
HO
OH
OH
OH
OH
glucose
OH
H
H
OH
H
OH
CH2OH
glucose
reversed in
galactose
Ribose
Found in DNA and RNA (FOX fig 2.29)
Found in ATP (FOX fig 4.15)
Found in NADH and FADH2 (FOX fig 4.17)
OH
HOH2C
O
HO
OH
ribose
removed in DNA
Disaccharides
(FOX fig 2.15)
Disaccharide short hand
Sucrose = glu-fru
Lactose = glu-gal
Maltose = glu-glu
What’s this?
glu-glu-glu-glu-glu-glu-glu-glu-glu-
Polysaccharide
glu-glu-glu-glu-glu-glu-glu-glu-glu Starch
Glycogen
linear chains of glucose
found in plants
densely branched chains of glucose
found in humans
Cellulose
chains of glucose (tend to stack into sheets)
found in plants
Why can’t we digest cellulose?
First how do we digest starch?
Amylase (enzyme) takes long chains of
glucose and breaks off disaccharide pieces.
What are the characteristics of enzymes?
Enzymes
Biological catalysts
either make reactions happen
or make reactions happen faster
Names end in –ase
starch (aka amylose) is digested with amylase
Can be classified according to activity
phosphatase – removes phosphate groups
kinase – adds phosphate groups
Proteins
Characteristics of Protein Interactions
Such as enzyme/substrate or receptor/hormone
Binding site that is specific
The substrate/hormone is called the ligand
(The ligand is the thing that binds to the protein)
What is the ligand for the aldosterone receptor?
What is the ligand for amylase?
The rate of reaction or activity is dependent
on binding characteristics.
Binding characteristics
Specificity – binding site designed for one
type of ligand
Affinity – strength of bond between ligand
and binding site
Competition – two or more ligands
competing for one binding site
Saturation – occupation of binding sites
thousands
of enzymes/receptors per cell
graph (FOX fig 4.6)
Saturation
(FOX fig 4.6)
Why can’t we digest cellulose?
starch has alpha linkages
cellulose has beta linkages
Example of
ENZYME
SPECIFICITY!!
Functions of Carbohydrates
Fuel
Signaling Molecule
Ribose is component of:
DNA RNA
ATP
NAD/FADH
Digestive Regulation
Fiber normalize transit time
Fiber decreases cholesterol, TAG and LDL