chemistry-class-12-unit-14-chapter-08-biomolecules-l-8-12-o1iogsxwppm

<p><Success style="float:center;text-align:center;font-size:28px;"> <B>Biomolecules Lecture-8</B></Success></p>
<p><primary style="float:center;text-align:center;font-size:24px;"> <B>Question</B></primary></p>
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<p><strong>Question-</strong> How to determime the primary structure of a polypeptide or a Protein?</p>
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<p><strong>Answer-</strong> Breaking the disulfide bridges -</p>
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<p>Reduce the disulfide bridges in order to obtain a single polypeptide chain</p>
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<p>We will achive this transformation by applying a reducing agent 2-mercaptoethanol</p>
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<p><img alt="image" src="/subject-images/iitpal/image/chemistry-class-12-unit-14-chapter-08-biomolecules-l-8_12-o1iogsxwppm-021-0362.4.jpg"></p>
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<footer style="font-size:18px;"> <span style="color:blue">Question</span> $\rightarrow$ Molecule with the disulfide bridges $\rightarrow$ Determining the number and kinds of amino acids $\rightarrow$ Secondary structure $\rightarrow$ α-helix $\rightarrow$ β-pleated sheet </footer>

<p><Success style="float:center;text-align:center;font-size:28px;"> <B>Biomolecules Lecture-8</B></Success></p>
<p><primary style="float:center;text-align:center;font-size:24px;"> <B>Determining the number and kinds of amino acids</B></primary></p>
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<p>To determine the number and kinds of amino acids in polypeptide chain, it was dissolved in 6M HCl and heated at $100^o \mathrm{C}$ for 24 hours</p>
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<p>Polypeptide $\xrightarrow[100^oC \hspace{1mm} 24hr]{6M \hspace{1mm} HCl}$ amino acids</p>
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<p>The mixture of amino acid is passed an amino acid analyzer to identify the amino acid</p>
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<p><img alt="image" src="/subject-images/iitpal/image/chemistry-class-12-unit-14-chapter-08-biomolecules-l-8_12-o1iogsxwppm-094-0834.0.jpg"></p>
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<footer style="font-size:18px;"> Question $\rightarrow$ Molecule with the disulfide bridges $\rightarrow$ <span style="color:blue">Determining the number and kinds of amino acids</span> $\rightarrow$ Secondary structure $\rightarrow$ α-helix $\rightarrow$ β-pleated sheet </footer>

<p><Success style="float:center;text-align:center;font-size:28px;"> <B>Biomolecules Lecture-8</B></Success></p>
<p><primary style="float:center;text-align:center;font-size:24px;"> <B>Secondary structure</B></primary></p>
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<div style='float: left; width:100%;font-size:22px;text-align:left'>
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<p>Secondany structure describes the repetitive conformations assumed by segments of the backbone chain of a polypeptide or a protein</p>
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<p>In other words secondary structure describes how segments of the backbone fold. Three factors determine the secondary structure of a segment of a protein</p>
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<p><img alt="image" src="/subject-images/iitpal/image/chemistry-class-12-unit-14-chapter-08-biomolecules-l-8_12-o1iogsxwppm-131-1168.8.jpg"></p>
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</main>
<hr>
<footer style="font-size:18px;"> Question $\rightarrow$ Molecule with the disulfide bridges $\rightarrow$ Determining the number and kinds of amino acids $\rightarrow$ <span style="color:blue">Secondary structure</span> $\rightarrow$ α-helix $\rightarrow$ β-pleated sheet </footer>

<p><Success style="float:center;text-align:center;font-size:28px;"> <B>Biomolecules Lecture-8</B></Success></p>
<p><primary style="float:center;text-align:center;font-size:24px;"> <B>Secondary structure</B></primary></p>
<hr>
<main>
<div style='float: left; width:100%;font-size:22px;text-align:left'>
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<p>The regional planarity about each peptide bond (as a result of  the partial double bond character of the amide bond), which limits the possible conformation of the peptide chain</p>
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<p>Minimizing energy by maximizing the number of the hydrogen bonds between peptide groups (that is hydrogen bond between carbonyl oxygen of one amino acid and the amide hydrogen of another)</p>
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<p><img alt="image" src="/subject-images/iitpal/image/chemistry-class-12-unit-14-chapter-08-biomolecules-l-8_12-o1iogsxwppm-175-1358.4.jpg"></p>
</div>
</main>
<hr>
<footer style="font-size:18px;"> Question $\rightarrow$ Molecule with the disulfide bridges $\rightarrow$ Determining the number and kinds of amino acids $\rightarrow$ <span style="color:blue">Secondary structure</span> $\rightarrow$ α-helix $\rightarrow$ β-pleated sheet </footer>

<p><Success style="float:center;text-align:center;font-size:28px;"> <B>Biomolecules Lecture-8</B></Success></p>
<p><primary style="float:center;text-align:center;font-size:24px;"> <B>Secondary structure</B></primary></p>
<hr>
<main>
<div style='float: left; width:60%;font-size:22px;text-align:left'>
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<p>Hydrogen bonding between peptide group</p>
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<p>The need for adequate seperation between neighbouring $R$ groups to avoid steric strain and repulsion of like charges</p>
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<img src="https://imagedelivery.net/YfdZ0yYuJi8R0IouXWrMsA/9566e890-ab7c-4f64-edae-047d01b19e00/public" width="90%">

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</main>
<hr>
<footer style="font-size:18px;"> Question $\rightarrow$ Molecule with the disulfide bridges $\rightarrow$ Determining the number and kinds of amino acids $\rightarrow$ <span style="color:blue">Secondary structure</span> $\rightarrow$ α-helix $\rightarrow$ β-pleated sheet </footer>

<p><Success style="float:center;text-align:center;font-size:28px;"> <B>Biomolecules Lecture-8</B></Success></p>
<p><primary style="float:center;text-align:center;font-size:24px;"> <B>α-helix</B></primary></p>
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<p>In $\alpha$-helix, the backbone of the polypeptide coils around the long axis of the protein molecule</p>
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<p>Because the amino acid have the L- configuration the $\alpha$-helix is a right handed helix, that is it rotates in a clock wise direction as it spiral down</p>
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<p>Each turn of the helix in contains 3.6 amino acids, and the repeat distance of the helix is $5.4 \mathrm{A^\circ}$</p>
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<img src="https://imagedelivery.net/YfdZ0yYuJi8R0IouXWrMsA/a9b8abd1-dc4c-4aa6-89c8-03829df3fd00/public" width="40%">

</div>
</main>
<hr>
<footer style="font-size:18px;"> Question $\rightarrow$ Molecule with the disulfide bridges $\rightarrow$ Determining the number and kinds of amino acids $\rightarrow$ Secondary structure $\rightarrow$ <span style="color:blue">α-helix</span> $\rightarrow$ β-pleated sheet </footer>

<p><Success style="float:center;text-align:center;font-size:28px;"> <B>Biomolecules Lecture-8</B></Success></p>
<p><primary style="float:center;text-align:center;font-size:24px;"> <B>β-pleated sheet</B></primary></p>
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<p><strong>$\beta$-pleated sheet:-</strong></p>
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<p>The hydrogen bonding in a $\beta$-pleated sheet occurs between neighbouring peptide chain</p>
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<img src="https://imagedelivery.net/YfdZ0yYuJi8R0IouXWrMsA/578fb4be-d285-489a-167d-9a06f161cd00/public" width="80%">

</div>
</main>
<hr>
<footer style="font-size:18px;"> Question $\rightarrow$ Molecule with the disulfide bridges $\rightarrow$ Determining the number and kinds of amino acids $\rightarrow$ Secondary structure $\rightarrow$ α-helix $\rightarrow$ <span style="color:blue">β-pleated sheet</span> </footer>

<p><Success style="float:center;text-align:center;font-size:28px;"> <B>Biomolecules Lecture-8</B></Success></p>
<p><primary style="float:center;text-align:center;font-size:24px;"> <B>β-pleated sheet</B></primary></p>
<hr>
<main>
<div style='float: left; width:100%;font-size:22px;text-align:left'>
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<p>A $\beta$-pleated sheet is almost fully extended the average two amino acid repeat distance is $7.0 \mathrm{A^\circ}$</p>
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<p>The part of the backbone structure of a protein background that exist in a pleated sheet is indicated by a flat arrow pointing in the $N \rightarrow C$ direction</p>
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<p>Silk, contains a large proportion of relatively small amino acid and therefore has large sagment of  $\beta$-pleated sheet</p>
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<p><img alt="image" src="/subject-images/iitpal/image/chemistry-class-12-unit-14-chapter-08-biomolecules-l-8_12-o1iogsxwppm-351-2666.4.jpg"></p>
</div>
</main>
<hr>
<footer style="font-size:18px;"> Question $\rightarrow$ Molecule with the disulfide bridges $\rightarrow$ Determining the number and kinds of amino acids $\rightarrow$ Secondary structure $\rightarrow$ α-helix $\rightarrow$ <span style="color:blue">β-pleated sheet</span> </footer>

<p><Success style="float:center;text-align:center;font-size:28px;"> <B>Biomolecules Lecture-8</B></Success></p>
<p><primary style="float:center;text-align:center;font-size:24px;"> <B>β-pleated sheet</B></primary></p>
<hr>
<main>
<div style='float: left; width:100%;font-size:22px;text-align:left'>
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<p>The number of side - by - side stands ranges from 2 to 15 in a globular protein the average stand in a $\beta$ - pleated sheet section contain six amino acids</p>
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<p>Wool and fibrous protein of muscles $\alpha$ helix</p>
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<p>$\beta$- Pleated sheet ${-}$ silk and spider web, it cannot be stretched</p>
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<p><img alt="image" src="/subject-images/iitpal/image/chemistry-class-12-unit-14-chapter-08-biomolecules-l-8_12-o1iogsxwppm-397-2955.6-2.jpg"></p>
</div>
</main>
<hr>
<footer style="font-size:18px;"> Question $\rightarrow$ Molecule with the disulfide bridges $\rightarrow$ Determining the number and kinds of amino acids $\rightarrow$ Secondary structure $\rightarrow$ α-helix $\rightarrow$ <span style="color:blue">β-pleated sheet</span> </footer>