Lecture 3, Protein folding and degradation with movie

Lecture 3, Protein folding and degradation with movie -...

Info iconThis preview shows pages 1–11. Sign up to view the full content.

View Full Document Right Arrow Icon
Lecture 3 Protein Folding, Degradation ***OPTIONAL READING: review article*** Goldberg, Elledge & Harper. (2001) The Cellular Chamber of Doom. Scienti±c American 284 :68-73. Downloadable @ blackboard
Background image of page 1

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

View Full DocumentRight Arrow Icon
The folding of a protein is controlled by its amino acid sequence Figure 3-5 Molecular Biology of the Cell (© Garland Science 2008)
Background image of page 2
4 0 Structure = formed when two or more polypeptide chains specifically bind each other. Alpha-helical coiled-coil often promotes the association of two proteins Figure 3-9 Molecular Biology of the Cell (© Garland Science 2008)
Background image of page 3

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

View Full DocumentRight Arrow Icon
The folding of a protein is controlled by its amino acid sequence • Some proteins fold on their own • Most proteins need help to fold properly
Background image of page 4
Most properly folded proteins (that have associated with appropriate partner proteins) do NOT have sizable exposed patches of hydrophobic amino acids on its surface. Figure 3-5 Molecular Biology of the Cell (© Garland Science 2008)
Background image of page 5

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

View Full DocumentRight Arrow Icon
Few proteins can refold on their own after complete denaturation Figure 3-6a Molecular Biology of the Cell (© Garland Science 2008)
Background image of page 6
Most proteins begin to fold as they are synthesized Figure 6-84 Molecular Biology of the Cell (© Garland Science 2008)
Background image of page 7

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

View Full DocumentRight Arrow Icon
Nascent proteins fold (often quickly) into an initial structure that then matures into the Fnal conformation Molten globule (dynamic and ±exible state) Mature conformation Figure 6-83 Molecular Biology of the Cell (© Garland Science 2008) Adjustment of side chain interactions
Background image of page 8
Some proteins require the binding of cofactors (e.g., Zn ++ ), other proteins and/or covalent modiFcations to fold into their mature conformation. Figure 6-82 Molecular Biology of the Cell (© Garland Science 2008)
Background image of page 9

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

View Full DocumentRight Arrow Icon
pathways for a protein Figure 6-85 Molecular Biology of the Cell (© Garland Science 2008) For many proteins, (molecular) chaperones assist in the folding process very early on (e.g., at the ribosome). Chaperones function, at
Background image of page 10
Image of page 11
This is the end of the preview. Sign up to access the rest of the document.

This note was uploaded on 09/19/2011 for the course BIO 320 taught by Professor Staff during the Spring '08 term at University of Texas.

Page1 / 33

Lecture 3, Protein folding and degradation with movie -...

This preview shows document pages 1 - 11. Sign up to view the full document.

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