Biomolecules Flashcards
Biochem and what are biomolecules
branch of chemistry that deal with molecules involving living systems. Carbohydrates, proteins vitamins nucleic acids
Carbohydrates formula Types of carb.
c6h1206 glucose and fructose . Monosacchardies, oligosacchardies, polysacchardises
Monosacchardides
A carb that cant be hydrolised further to give simpler polohydroxy ald or ketone eg glucose
Oligosaccharides
Carbs that produce 2 to 10 monosacchardies on being hydrolised . eg sucrose
Polysaccharides
Crabs that prodduce a large number of monosac. on hydrolisis . eg startch, cellulose called non sugars
reducing sugars and non reducing sugars
carbs which can reduce tollns reagent and fehlings reagent are called reducing sugars . vice versa
Aldose
Monosaccharidees having aldehyde. eg glucose
ketose
monosaccharides having ketone fructose
Glucose preparation
from sucrose ( hydrolysis ) [c12h22o11] from startch ( ") [C6H10O5]n
Glucose structure and 5 evidence to show linear
Linear structure
a) 6 carbons in straight chain
b) presence of carbonyl grp (CO )
c) Presence of aldhyde
d) presence of 5 Oh grp
e) presence of 1degree alchoholic grp
Haworth Projection
Six membered cylic structure of glucose
Anomers
Isomers that differ in the config at acetal or hemiacetal carbon atoms of a sugar in cyclic form. eg. alpha-d-glucose and beta-d-glucose
Cyclic glucose evidence 3
despite having aldehyde grp they do not give 2,4-dnp test.
pentaacetate of glucose does not react with Nh2-Oh indicating the absense of free -cho group
Glucose is found in two forms called alpha and beta. they both have different boiling and melting points
Amino Acids made of
Amino Grp and carbocyl grp
Amino acids on the basis of nature of synthesis
non essential/ essential
Non essential Amino acids- amino acids that can be synthethised in the body . eg glycerin
esesntial amino acids can not be synthesided in the body and must be obtained through diet
Amino acids on the basis of functional grp
a] neutral aa- one nh2 and one cooh grp eg gylcerin
b] acidic aa- one nh2 and 2 cooh grp aspartic acid
c] basic aa- more no of nh2 than cooh
Zwitter Ion
Due to the presence of acididc and badic groups in the same molecule, in aques solution cooh grp loses proton and nh2 grp accept proton giving rise to a dipolar ion called zqitter ion.
it can react with both acid and bases so its amphoteric in nature.
Proteins
wht is peptide bond
Dipeptide, tri, poly
Polymers of alpha amino grp and they are connected to each other by peptide bond.
Peptide linkage is formed bw one cooh grp of one alpha-amino acid and -nh2 grp of another amino acid by loss of water molecules
combination of 2/3/many amino acids by peptide bond
Fibrous and globular proteins
Fibrous Proteins- polypeptide chains run parralel and held together by hydrogen and di sulphide bonds
eg. keratin[hair,wood]
Globular proteins polypeptide coil around a spherical shape
eg. insulin
primary structure of proteins
one of more polypeptide chains may be present. each polypeptide chain in a protein linked togetgher in a specific sequence of amino acids
2 degree structure of protin explain alpha helix and b sheet
shape in which long polypeptide chain can exist. they exist in two different structure, alpha helix and beta sheet
a] alpha-helix-
most common ways in which polypeptide chain forms all possible hydrogen bonds by twisting into helix. this hydrogen bond is between -nh- grp of each amino acid to -co- grp of adjacent turn of helix
b] beta sheet
all peptide chains are strecthed out to maximum extent and then laid side by isde
tertiary structure of proteins
formed by further folding of secondary structure. gives rise to fibre and globular structure
Quaternary Structure of protein
the spatial arrangement of units of proteins with respect to each other
Denaturation Of protein
When a native form of protein is subjected to physical or chemical change, hydrogen bonds are disturbed.
Due to this unfolding of helix protein and protei loses its biological activity.
During denaturation 2degree/3 are destroyed but 1 degree remain intact
