intro Flashcards
how many types of AAs are there
20- all have a similar structure
what sets AAs apart from each other and how do these differences alter function
differences in side chains cause hydrophobism and hydrophilia. they also ionise the AAs
define primary structure
the initial sequence chain of AAs coding for a protein
define secondary structure
the primary structure folds into alpha helixes and beta sheets
define tertiary structure
the overall 3D shape of a protein
define quaternary structure
a protein composed of different tertiary subunits
what is an eg of a quaternary structure
a RBC- they have 4 Hb subunits
give 4 examples of structural proteins
- keratin
- chitin
- collagen
- cartilage
where would keratin be found
hair and nails
where would collagen be found
connective tissue and skin
where would chitin be found
insect shells
where would cartilage be found
nose, ears and shark fins
give 3 examples of functional proteins
- venom toxins
- channel proteins
- enzymes
give an example of a venom toxin
bungarotoxin- found in snakes
give an example of a channel protein
ion channel (used to transport ions along their concentration gradient)
give and example of an enzyme
amylase- used to aid digestion
what is a Q value
the value used to show the effect of temperature on a reaction
how is a Q value calculated
Q10= Rt/Rt(-10)
what does Q10 stand for in the Q10 equation
the rate of reaction with a 10ºC increase
what does the first Rt stand for in the Q10 equation
the base reaction rate
what does Rt(-10) stand for in the Q10 equation
the reaction rate at a temperature -10ºC to that of the base rate
what is the composition of ATP
adenosine, ribose (5c), phosphate (3)
how is energy released from ATP
high energy and between the phosphates is broken
where does glycolysis take place
in the cytoplasm