cellular molecules Flashcards
define proteins
large, complex molecules that play many critical roles in body
describe various classes of amino acids
non-polar
polar
acidic
basic
describe functions of proteins
repair and build body’s tissues
allows metabolic reactions to take place
coordinates bodily functions
primary structure of proteins
amino acid sequence
polypeptide sequence
secondary structure of proteins
formed by H bonds between carbonyl and amino groups that make up the polypeptide backbone
alpha helices, beta sheets and random coil
tertiary structure of proteins
overall 3D arrangement of its polypeptide chain in space
quaternary structure of proteins
association of several protein chains or subunits into a closely packed arrangement
subunits held together by H bonds and van der Waals forces between nonpolar side chains
what properties may quaternary structure confer on proteins?
two or more identical or different polypeptide chains
globular v fibrous proteins
fibrous = long, narrow strands , helical like structure, generally structural roles - only soluble in strong acids globular = compact, rounded shape, folded ball like structure, functional roles - soluble in water, acids and bases
examples of globular
haemoglobin,
insulin,
myoglobin, immunoglobulins
and many enzymes
examples of fibrous
keratin
collagen
elastin
fibroin
explain denaturation
primary structure is unaffected, however, shape of protein can be altered so much that the protein becomes dysfunctional = therefore protein considered denatured
this can happen when protein is subject to changes in temp, pH, chemical exposure etc outside optimal range
glycoprotein - what molecules
carbohydrate and protein
lipoprotein - what molecules
lipid (fat) and protein
elastins
ECM protein , fibrous protein function - extensibility and elastic recoil of many vertebrate tissues eg arteries, valves, skin etc
keratins
fibrous structural proteins
main constituents of hair, nails etc
produced by keratinocytes (stratum corneum layer, outermost layer of skin - regenerative)
functions - protect epithelial cells, strengthen internal organs, control growth of epithelial cells, maintain elasticity
define enzymes
biological catalysts, proteins which help speed up metabolism or the chemical reactions in our bodies
naturally produced but can be manufactured
how do enzymes catalyse reactions
enzyme binds to substrate(s) on the active site, substrate molecule changed -> product formed
lowering activation energy necessary for a reaction to occur
discuss rate of an enzyme-catalysed reaction - factors etc
temperature - ^temp, ^rate - however extreme temps can cause denaturation
pH - optimum range, extreme values cause denaturation
enzyme conc - ^conc, ^rate
substrate conc - ^conc, ^rate
define Michaelis constant and explain
describe molecular nature of competitive inhibition
competitive inhibitors bind to enzyme, often at active site, which prevents real substrate from binding , therefore , inhibitor and substrate compete for enzyme
decreases no. of enzyme molecules available to bind to substrate
describe molecular nature of non-competitive inhibition
inhibitor doesn’t prevent substrate from binding , inhibitor and substrate do not affect each other’s binding
however, when inhibitor is bound, enzyme cannot catalyse its reaction to produce a product
decreases no. of functional enzyme molecules that can carry out reaction