Lect6 - Folding information in primary sequence of proteins...

Info iconThis preview shows pages 1–23. Sign up to view the full content.

View Full Document Right Arrow Icon
Background image of page 1

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

View Full DocumentRight Arrow Icon
Background image of page 2
Background image of page 3

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

View Full DocumentRight Arrow Icon
Fig. 4-27 Lehn
Background image of page 4
Fig. 4-27 Lehn
Background image of page 5

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

View Full DocumentRight Arrow Icon
Fig. 6-2 B and T
Background image of page 6
Molten Globule Final folded form
Background image of page 7

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

View Full DocumentRight Arrow Icon
Fig. 6-5 B and T
Background image of page 8
Fig. 4-29 Lehn
Background image of page 9

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

View Full DocumentRight Arrow Icon
Fig. 4-28 Lehn
Background image of page 10
Crowded cytoplasm (tRNA in blue, ribosomes in green, proteins in red)
Background image of page 11

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

View Full DocumentRight Arrow Icon
Background image of page 12
Molecular Chaperones function analogously to human counterparts: “They inhibit inappropriate interactions between potentially complementary surfaces and disrupt unsuitable liasons so as to facilitate more favorable associations” John Ellis
Background image of page 13

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

View Full DocumentRight Arrow Icon
General Features of Chaperones Proteins that catalyze the folding of other proteins
Background image of page 14
Background image of page 15

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

View Full DocumentRight Arrow Icon
Background image of page 16
Background image of page 17

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

View Full DocumentRight Arrow Icon
Background image of page 18
Background image of page 19

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

View Full DocumentRight Arrow Icon
Background image of page 20
Background image of page 21

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

View Full DocumentRight Arrow Icon
Background image of page 22
Background image of page 23
This is the end of the preview. Sign up to access the rest of the document.

Unformatted text preview: Folding information in primary sequence of proteins But, cellular concentration of proteins ~300 mg/ml Aggregation Rate of chain elongation is ~ 4 amino acids/second, so about ~ 4 minutes for a 1000 residue protein Exposed hydrophobics Initially identified as proteins induced by heat shock heat shock proteins (Hsp) Fig. 3-19 Lehn Fig. 3-19 Lehn Fig. 3-20 Lehn Fig. 3-20 Lehn...
View Full Document

This note was uploaded on 10/05/2009 for the course BIBC 100 taught by Professor Nehring during the Winter '07 term at UCSD.

Page1 / 23

Lect6 - Folding information in primary sequence of proteins...

This preview shows document pages 1 - 23. Sign up to view the full document.

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