Biomolecules Flashcards

1
Q

Biochem and what are biomolecules

A

branch of chemistry that deal with molecules involving living systems. Carbohydrates, proteins vitamins nucleic acids

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2
Q

Carbohydrates formula Types of carb.

A

c6h1206 glucose and fructose . Monosacchardies, oligosacchardies, polysacchardises

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3
Q

Monosacchardides

A

A carb that cant be hydrolised further to give simpler polohydroxy ald or ketone eg glucose

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4
Q

Oligosaccharides

A

Carbs that produce 2 to 10 monosacchardies on being hydrolised . eg sucrose

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5
Q

Polysaccharides

A

Crabs that prodduce a large number of monosac. on hydrolisis . eg startch, cellulose called non sugars

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6
Q

reducing sugars and non reducing sugars

A

carbs which can reduce tollns reagent and fehlings reagent are called reducing sugars . vice versa

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7
Q

Aldose

A

Monosaccharidees having aldehyde. eg glucose

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8
Q

ketose

A

monosaccharides having ketone fructose

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9
Q

Glucose preparation

A
from sucrose ( hydrolysis ) [c12h22o11]
from startch ( ") [C6H10O5]n
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10
Q

Glucose structure and 5 evidence to show linear

A

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

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11
Q

Haworth Projection

A

Six membered cylic structure of glucose

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12
Q

Anomers

A

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

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13
Q

Cyclic glucose evidence 3

A

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

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14
Q

Amino Acids made of

A

Amino Grp and carbocyl grp

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15
Q

Amino acids on the basis of nature of synthesis

non essential/ essential

A

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

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16
Q

Amino acids on the basis of functional grp

A

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

17
Q

Zwitter Ion

A

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.

18
Q

Proteins
wht is peptide bond
Dipeptide, tri, poly

A

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

19
Q

Fibrous and globular proteins

A

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

20
Q

primary structure of proteins

A

one of more polypeptide chains may be present. each polypeptide chain in a protein linked togetgher in a specific sequence of amino acids

21
Q

2 degree structure of protin explain alpha helix and b sheet

A

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

22
Q

tertiary structure of proteins

A

formed by further folding of secondary structure. gives rise to fibre and globular structure

23
Q

Quaternary Structure of protein

A

the spatial arrangement of units of proteins with respect to each other

24
Q

Denaturation Of protein

A

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

25
Q

Native Protein

A

protein found in biological system with unique 3d arrangement

26
Q

chemical composition of Nucleic ACId

A

nucleic acid + hydrolysis= pentose sugar + phosphoric acid + base

27
Q

RNA composition

A

beta-D-deoxyribose + phosphoric acid + agct

28
Q

DNA composition

A

Beta-D-ribose +phosphoric acid + AGCU

29
Q

Double Strand Helix structure for DNA

A

the two strands are complimentry to each other bcoz the hydrogen bonds are formed bw specific pairs of bases.
Adenine forms hb with thymine
cytosine forms hb with guanine

30
Q

RNA molecules are of 3 types

A

messenger RNA
ribosomal rna
transfer rna

31
Q

function of dna

A

dna is the chemical basis of heredity and may be regarded as reserve of gentic info.

32
Q

function of nucleic acid

A

protein synthesis in the cell