NOTES
Topic/Objective:
Proteins -
many
Name: Ivan Li
Date: Sept 28 2023
structures & Functions ,
Class/Period: SBIUUI/ Perical 4
Essential Question: What is a
protein ,
why is it important ,
Questions & Cues Notes
Study examp lesI Protein-proteins meaning First Place
explanations of Account for 50% of
structural
dry weight : most cells
now pro Leins -used for support ,
transport torage sigwalling
,
S
, through organism ,
userI
& of her stances
are movement defense
against foreign sub ,
chemical
for these -
regulate metabolism ,
can -ly
selecte accelerate reactions on a well
.
fencpods .
humans have fews of thousands of different problems
each has a different structure & function .
most
structurally sophisticated molecule known
All proteins are
polymers made of the same 20 amino acids .
polymers of atam &
a
rop Mino group carboxy group
chain
Chyctogen
variable Sick
a
R is different
g amino acid
-
in every .
Can be
simple (glycine) or
complex (glutamine)
Amino acids can be polar , non-polar .
-
negative side chain are to carboxyl groups
:
acidic
-Basic amino aids have amino
groups in the side chain generally positive
in
charge :
Amino acids Can link through dehydratio reaction ,
covalent le bond
causing peptic a .
-many pephile beads elike) yields a polypeptice
↓ of many
fome linked
lend i polymer
-
amino other ac bond
.
is a free grop
carboxyl
/
amino
grop .
by Peptic
Summary
polypeptide
eleebond
te
Amino
backbone
polypephicle
NOTES
Topic/Objective: Name:
Date:
Class/Period:
Essential Question:
Questions & Cues Notes
-repeated sequence =
polypeptide backbone .
-each
polypeptic is a
unique sequence of amino acis's
sequence of amino acials decide shape of protein
-
-
-function of protein depend on
to
its ability recognize &
bind to another molecule .
4 Levels of Protein structure :
-
Primary
-
secondary
-
tertiary
~
Quaternary
primary unide strucker of amino
:
acic
,
small variations ic can cause
disorders Eie sickter cell diseases
segmenpeatedly
secondary overall
:
coild or folded in
patterns ,
conforma /On
~only backbone involved , not amino side
chains .
-chelix-coil shape .
-
pleated sleet -
two or more hie parallel to eachother
regrou
.
Merliary iregular can tortione from sich chain interactions
:
,
hydrophobic interaction , polypeptide folds into
a functional conformation , non-polar sides end
up
water
at of protein contact with
.
core , no
Summary
primary -> Secondary -echoy -
quatuary
NOTES
Topic/Objective: Name:
Date:
Class/Period:
Essential Question:
Questions & Cues Notes
Disulfiche bridges - Gocysteine monomers with 7-st side chairs
close protein
are brought by folding
.
Rink part of protein together .
Qualenary structure -
two or more polypiphile chains
aggregated into one factional macromolecules
g
.
c .
collagen
,
coils into triple belix
Denaturation -
protein may
unravel & low it native conformation .
Summary
