 ौ ौ ौ ौ ौ ौ ौ ौ ौ ौ ए gü हूॆ ौ ौ 好ृ,verage structure contest ौ ौ ौ Stuff, students, if we talk about , ौ They are at the third level of protein accountability cientoa Layer Protection ौ Indians �好吃 भीआत of the second structure आप दपोलीकबटर short structure आप पुरीól प्रप्रने काए काए तोभगों थोत होझा the whole polypeptide chain अखथे fold on the whole poly-peptide chain की अखथे fold on the whole अगँँँँँँँँँँँँँ यह the whole poly-peptide chain अखचचचृ बरे प्रप्रने काए वो। over or folding off अप पूलि प्रप्तार चैन तौद तुद दिमनेशन्छल फाम यक अबरालग त्फोल्ड होगा गे तुद दिमनेशन्छल प्रपर शेप तेठ गी प्रुटीन तुद विसकमदबग़ाइसका तरस्च्चेट श्क्चर कहेंगे there are different types of bonds which are involved in tertiary structures tertiary structures main different types of bonds are involved in which there are hydrogen bonds, ionic bonds, hydrophobic interactions and disulfide bonds, here if we see hydrogen bonds then you are understanding that one is the hydrogen of the amino acid and the other is the oxygen of the amino acid and you have come in front of me to make a hydrogen bond ionic bonds, now because some amino acids are like this if the negative charge of the amino acid comes in front of the positive charge of the amino acid then the bond between the negative and the positive charge is the ionic bond hydrophobic interaction is very very interesting there are some amino acids which are repellent of water we call them as hydrophobic amino acids now when any protein, because cell environment is an aquatic environment water environment, the hydrophobic amino acids try themselves to fill the protein molecule so the protein which is not in the cytoplasm of the cell the amino acids try to come in between the hydrophobic amino acid so that they can cover the vacuum amino acid from outside and not reach the water when many amino acids, because there will be many hydrophobic amino acids in the protein when they are big, then the interaction between them develops these disulfide bonds are also present in the tertiary structure of proteins in every protein, when there is a fold up of a tertiary structure then after primary and secondary there is a tertiary structure some proteins are like this which are made up of only one polypeptide chain the only polypeptide chain which is made up of only one polypeptide chain then the tertiary structure is retained the final structure is the tertiary structure for kidney proteins, they have one polypeptide chain the polypeptide chain is made up of only one polypeptide chain after tertiary, they are made up of quaternary structure so their final structure is not a tertiary structure but a fold up so here we have the myoglobin if we see that the oxygen from the hemoglobin has to reach the tissues and cells which are present in the muscles so myoglobin consists of one polypeptide chain so its final structure is the tertiary structure this is the amylase the saliva amylase i.e. the carbohydrate digesting enzyme in the saliva which is typically called Tylane that is also made up of one polypeptide chain so the Tylane or amylase is also made up of one polypeptide chain and its final or functional structure that will be a tertiary structure