NON - polypeptide chain causing a sharp transition in the...

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NON-POLAR NEUTRAL The NON-POLAR NEUTRAL amino acids are HYDROPHOBIC (water- repelling). There are 10 amino acids with hydrophobic side chains. They tend to interact with one another and with other hydrophobic groups and would be expected to be located within the interior of a protein or in membranes. Typically they have primarily C and Hs in the R group. The simplest of course is glycine , which has a single H as its side group: alanine, valine, leucine, and isoleucine have hydrocarbon chains consisting of up to 4 carbon atoms. Proline also contains a hydrocarbon side chain but it forms a ringed structure: As a result, a proline residue disrupts the usual organization of the backbone of a
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Unformatted text preview: polypeptide chain, causing a sharp transition in the direction of the chain. The presence of proline, therefore, interrupts the formation of any regular repeating structure. The side chains of cysteine and methionine contain sulfur atoms. Methionine is very hydrophobic, cysteine is less so. Even though both contain sulfur atoms, only cysteine can form disulfide bonds. Phenylalanine and tryptophan both have side chains containing very hydrophobic aromatic rings. These amino acids can participate in ring stacking....
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This document was uploaded on 11/03/2011 for the course BIOLOGY MCB2010 at Broward College.

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