Sandbox 51: Difference between revisions

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The amino acids present in the lysozyme polypeptide sequence have a direct influence not only on primary structure, but also on the secondary structural changes as well as the tertiary structural changes which can be influence by polarity and charge of the sidechains. The various amino acid <scene name='Sandbox_38/Aminoi/1'>residues</scene> differ in their properties because of the great variety of side chains present on each amino acid. Polar and nonpolar, and charged and uncharged side chains lead to various degrees of hydrophobicity and hydrophilicity which can have a very dominant effect on protein folding. In lysozyme, these <scene name='Sandbox_38/Sc/1'>side chains</scene> are displayed for each amino acid residue.

Sandbox 51: Difference between revisions

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Revision as of 21:26, 5 March 2011 view source John Ripollone (talk \| contribs) 207 edits No edit summary ← Older edit		Revision as of 21:27, 5 March 2011 view source John Ripollone (talk \| contribs) 207 edits No edit summary Newer edit →
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	The amino acids present in the lysozyme polypeptide sequence have a direct influence not only on primary structure, but also on the secondary structural changes as well as the tertiary structural changes which can be influence by polarity and charge of the sidechains. The various amino acid <scene name='Sandbox_38/Aminoi/1'>residues</scene> differ in their properties because of the great variety of side chains present on each amino acid. Polar and nonpolar, and charged and uncharged side chains lead to various degrees of hydrophobicity and hydrophilicity which can have a very dominant effect on protein folding. In lysozyme, these <scene name='Sandbox_38/Sc/1'>side chains</scene> are displayed for each amino acid residue.		The amino acids present in the lysozyme polypeptide sequence have a direct influence not only on primary structure, but also on the secondary structural changes as well as the tertiary structural changes which can be influence by polarity and charge of the sidechains. The various amino acid <scene name='Sandbox_38/Aminoi/1'>residues</scene> differ in their properties because of the great variety of side chains present on each amino acid. Polar and nonpolar, and charged and uncharged side chains lead to various degrees of hydrophobicity and hydrophilicity which can have a very dominant effect on protein folding. In lysozyme, these <scene name='Sandbox_38/Sc/1'>side chains</scene> are displayed for each amino acid residue.