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Unformatted text preview: Globular Proteins Types of Interactions Nonpolar and Polar Hydrophobic (nonpolar) R groups tend to cluster in the interior of the protein structure away from water. The thermodynamic driving force for this separation is entropy . When nonpolar structures dissolve in water, a relatively rigid water structure forms around it. This higher ordered structure has low entropy and is energetically disfavored. About half of the R groups in amino acids are hydrophobic, and tend to be positioned in the interior of a globular protein. hydrophobic R groups CH 3- (CH 3 ) 2 CH- CH 3 CH 2 CH- CH 3 alanine valine isoleucine CH 3 CHCH 2- CH 3 CH 2- leucine phenylalanine Globular proteins derive their name from their spherical and more compact structure than fibrous proteins. The structure of globular proteins also is more complex with pleated sheets and helices accounting for about half of the secondary structure, with the remainder made up of loops where polypeptide chains fold back on themselves to produce the spherical shapes. This bending of the polypeptide chains is produce the spherical shapes....
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