3:25 anotherr are generally represented by a symbol
5:30 are asci
5:33 B depending upon the Rel number
5:56 molecule AMS are usually colorless cryst
5:58 solids these are water soluble high
6:01 melting solids and behave like salts
13:27 3.3 Ty
13:31 of different typ of Ty
14:49 inic form Amino show Behavior as they
15:01 acids and
15:04 bases so except gin all other naturally
15:06 occurring Alpha amino acids are
15:43 different they exist both in D and
15:56 uration are represented by writing the
16:14 next structure of prot
16:24 number you have already read that
16:27 proteins are the polymer of alamin
16:29 acids so they are connected to each
17:16 linkage is formed between Co group and
17:17 nh2 group the reaction between two
17:19 molecules of similar or different amino
17:21 acids process through the combination of
17:24 amino acid group amino group of one
17:27 molecule with the carox group of the
17:30 other the product the reaction is called
18:18 a polypeptide with more than 100 amino
18:20 acid residual having molecular mass
18:47 for example however the distinction
18:50 between polypeptide and a protein is not
19:00 with fewer amino acids are likely to be
19:04 called proteins if they ordinarily have
19:07 a well defined confirmation of proteins
19:35 if they ordar have a well defined
19:48 as so proteins can be classified into
19:50 two types on the Bas of their molecular
20:17 prot when the poly chains run paral and
20:20 are held together by hydrogen and dulf bonds
20:34 fiber like structure are formed such
20:41 water some common examples
20:53 in
20:56 glin glob prot this structure results
21:20 chap these are usually soluble in water
21:28 GL so insulin and alamin are the common
21:49 prot structure and shape of proteins can
21:52 be studied at four different levels struct
22:29 of prots may have one or more
22:32 polypeptide chains each polypeptide in a
22:34 protein has amino acids linked with each
22:37 other in a specified sequence and it is
22:39 the sequence of amino acid that is said
22:40 to be a primary structure of that
22:43 protein any change in this primary
22:46 structure that is the sequence ofat a
23:12 the second of protein refers to the
23:16 shape on in which a long poly can exist
23:18 they are found to exist in two different
23:22 types of structures alha hel then beta structure
24:46 this structure arise due to the regular
24:48 folding of backbone of the poly peptide
24:50 chain due to the hydrogen bonding
24:52 between Co and NH group in the peptide bond
25:15 is one of the most common ways in which
25:17 poly chain forms all possible hydrogen
25:20 bonds by twisting into a right-handed
25:22 screw right handed
25:26 screw hel with NH group and each am
25:28 resid hydrogen bonded to the co group of
25:30 turn of the Helix is shown figure
25:34 14.1 beta structureal pepti chains are
25:38 stretched out to nearly maximum
25:41 extension extension and then light side
25:43 by side which are held together by inter
25:49 bonds structure resembl the ple fls of
25:52 dra and therefore is known as betaed structure
26:12 the ter strcture of proteins represents
26:18 poly further folding of the secondary
26:20 structure it gives rise to the two major
26:22 molecular shape fibrous and glob the
26:24 main forces which stabilize the
26:27 secondary and structure of proteins are
26:30 hydrogen bonds d suide linkages vs and
26:33 electrostatic force of attraction in the
27:07 Force linkage hyrogen bonding elatic
27:09 force of attraction okay next structure of
27:28 protein of some of the protein are
27:31 composed two or more polypeptide chains
27:33 referred to as subunits the special
27:35 arrangement of these subunits with
27:38 respect to each other is known as quary structure
28:23 next biological system with
28:25 threedimensional structure and
28:26 biological activi is called native
29:11 Str when a protein in Native form is
29:13 subjected to physical change like change in
29:25 tempure distur due to this Globus unfold
30:51 natur so during secondary andure are
30:53 destroyed but it primary structure
31:22 theur another example is curling of milk
31:24 which is caused due to the formation of
31:25 lactic acid by the bacteria present in
31:45 next question melting points and
31:47 solubility in water of amino acids are
31:49 generally higher than that of
32:39 where does the water in theg go after
33:04 next en en
33:59 biolog for example the enzymes that
34:01 cataly hydrolysis of maltose into
34:03 glucose is named as
34:13 glucose
34:22 reaction for example the enzymes which
34:25 cataly the oxidation of one substrate
34:27 with the simultaneous reduction of
35:27 enes areed only in small quantities for
35:29 the progress of reaction similar to the
35:31 action of chemical Catalyst enzymes are
35:33 said to reduce the magnitude of
37:15 of while the activation energy is only
37:18 2.5 k per Mo when hydr by the
37:52 mechm of the enzy action has been discussed
38:45 but so organic compounds required in the
38:47 diet in small amount of perform to
38:49 perform specific biological functions
38:52 for normal maintenance of optimum growth
39:24 vitamin pills should not be taken
42:07 nuclic acids of the cell responsible for
42:09 the heridity are called chromosomes
42:11 which are made up of proteins and
42:12 another type of biomolecules called
42:15 nuclic acid okay so these are mainly two
42:18 types deoxy nucle acid and ribonucleic
42:21 acid since nucle acids are long chain
42:22 polymer of nucleotides
42:24 nucleotides
42:27 nuc poly long
43:16 ory comp DNA molecules the sugar is
43:21 beta2 deox where in RNA molecule it is
43:40 Nu so DNA contains four
43:44 bases Adine gine cytosin and thyine RNA
43:46 also contains four bases first three
43:50 bases are same as in DNA but the fourth
45:43 are joined together by phosph linkage
45:46 between five and three carbon atoms of
45:49 the Pento sugar the formation of typical
46:28 car and third carbon atoms of the Pento
46:32 sugar five and third carbon atom fifth
46:57 thir number Sulee phosphor
47:46 so information regarding the sequence of
47:48 nucleotides in the chain of the nucleic
47:55 structure nucle acids have a secondary
47:57 strcture also G and
47:58 and
48:15 standard standard structure for DNA two
48:17 nucle acid chains are wed about each
48:19 other and held together by hydrogen
48:26 bases the two stands are complimentary
48:28 to each other because the hydrogen bonds
49:33 second hel hel hel are present which are
49:35 only single
49:37 standard sometimes they fold back on
50:11 nuc
50:32 and what products would be formed when a
50:36 nucleo from DNA containing time in
50:38 hydrolyzed what product would be formed
50:41 when a nucleotide from DNA containing th
50:43 is hyd hyd
50:58 Beto th bet d thin
51:08 Deo
51:12 Deo then phosphoric acid phosphoric acid okay
51:23 next when RNA is hydrolyzed there is no
51:26 relationship among the quantities of
51:29 bases obtained what does this fact
