Lecture Notes 9-15-08 - Macromolecules in Cells Three...

Info iconThis preview shows pages 1–8. Sign up to view the full content.

View Full Document Right Arrow Icon

Info iconThis preview has intentionally blurred sections. Sign up to view the full version.

View Full DocumentRight Arrow Icon

Info iconThis preview has intentionally blurred sections. Sign up to view the full version.

View Full DocumentRight Arrow Icon

Info iconThis preview has intentionally blurred sections. Sign up to view the full version.

View Full DocumentRight Arrow Icon

Info iconThis preview has intentionally blurred sections. Sign up to view the full version.

View Full DocumentRight Arrow Icon
This is the end of the preview. Sign up to access the rest of the document.

Unformatted text preview: Macromolecules in Cells Three Families of Macromolecules Protein Folding Protein Folding The protein molecule can fold in an enormous number of ways However, protein folding is constrained by a number of forces: Noncovalent bonds (hydrogen and ionic bonds or van der Waals forces) can hold regions of a polypeptide chain together Clustering of hydrophobic and hydrophilic side chains The distribution of polar, non polar, and ionic amino acids is an important factor that dictates the particular low energy three-dimensional conformation of each folding protein All the information necessary for adopting the three-dimensional shape of the protein is contained in the linear amino acid sequence Amino acids are joined together to form a polypeptide backbone with attached side chains. It is the sequence of chemically different side chains that makes each protein distinct. There are an equal number of polar and nonpolar side chains....
View Full Document

Page1 / 19

Lecture Notes 9-15-08 - Macromolecules in Cells Three...

This preview shows document pages 1 - 8. Sign up to view the full document.

View Full Document Right Arrow Icon
Ask a homework question - tutors are online