CSB327H1 Lecture Notes - Lecture 3: Lysyl Oxidase, Matrix Metalloproteinase, Type I Collagen

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coraleel39

5 Jan 2013

School

UTSG

Department

Cell and Systems Biology

Course

CSB327H1

Professor

Maurice Ringuette

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Document Summary

Csb327 lecture 3 notes extracellular processing (september 17, 2012) 2 lecture outline: the next step is to look at extracellular fibrillogenesis that happens on the outside of the cell. You cleave the n- and c- pro-peptide within the matrix compartment but it is on the extracellular side of the cellular compartment. 3 cross-links formed between modified lysine side chains with a collagen fibril: you have two types of cross linking. You have intramolecular cross linking which is within the triple helix. You have intermolecular cross linking which is between c- terminal and n-terminal telopeptides. 4 side-by-side interactions between collagen molecules is stabilized by aldol cross-links between two lysine side chains. I will not ask you to re-draw lys residue. You can have cross linking in the telopeptide domain and to a lesser degree, within the triple helix of lys and ho-lys residues. The enzyme that does this is lysyl oxidase (lo).

Related Questions

1. The level of protein structure that is stabilized primarilyby non-covalent interactions between the side chains within asingle polypeptide chain is refered to as its:

A) primary structure

B) secondary structure

C) tertiary structure

D) quaternary structure

E) none of the above

2. Collagen, a strong fibrous protein found in connectivetissue, bone, and the extracellular matrix, has a structure inwhich three left-handed helices wind around each other to form aright-handed triple helix. The primary structure of collagen has arepeat unit of -(Gly-X-Pro)- Which of the following bonds stabilizethe collagen triple helix? (mark all that apply)

A) Hydrogen bonds between hydroxyproline residues

B) Hydrogen bonds between N-H and C=O

C) Ionic bonds between amino acid side chains

D) Hydrogen bonds between charged amino acids

3. The non-covalent forces that stabilize the Beta-strandconformation of peptides include:

A) H-bonds between amide C=O and amide NH

B) Van der Waals packing between the peptide backbone atoms

C) Van der Waals packing due to side chain interdigitation

D) Only A and B above

E) None of the above

4. What is the approximate length difference of a 22-kDasingle-stranded ?-helical protein segment vs. a 22-kDasingle-stranded ?-strand protein segment? Assume a mean residuemass of 110 Da. Show work.

5. Circular dichroism measurements have shown that the peptidebackbone of poly-l-lysine (KKKKKKK) adopts a random coilconformation at pH 7.0, but becomes ?-helical as the pH is raisedabove 10. This observation is known as the

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CSB327H1 Lecture Notes - Lecture 3: Lysyl Oxidase, Matrix Metalloproteinase, Type I Collagen

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