Lecture 4 - Protein Purification

Lecture 4 - Protein Purification - Biochem 415/515 -Lecture...

Info iconThis preview shows pages 1–13. Sign up to view the full content.

View Full Document Right Arrow Icon
Biochem 415/515 -Lecture 4 Continuation of Protein folding Protein purification Announcement Help sessions will start next week on Mondays 7-9 PM 5330 Med Sci 1
Background image of page 1

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

View Full DocumentRight Arrow Icon
Xu, Z. Horwich, A.L. Sigler, P.B. The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex. Nature v388 pp.741-750 , 1997 Crystal Structure of GroEL
Background image of page 2
Mechanism of GroEL Lin Z., Madan, D., Rye, H.S., Nat. Struct. Biol. (2008) 15, 303 ATP ADP GroES GroES + ATP GroES + ADP Pi Pi Pi GroES + ATP ~800 kDa GroEL GroES
Background image of page 3

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

View Full DocumentRight Arrow Icon
Certain neurological diseases result from misfolding of proteins Bovine Spongiform Encephalitis (BSE, mad cow disease) and Creutzfeldt-Jacob disease result from prion protein (PrP) aggregation in neural tissue Formation of amyloid fibers and plaques (from proteins like amyloid β and α- synuclein) contribute to neurodegenerative disorders, such as Alzheimers and Parkinsons Disease Plaques
Background image of page 4
Structure of the Amyloid Fibrils Formed by the Amyloid β Protein
Background image of page 5

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

View Full DocumentRight Arrow Icon
Acetylation, proteolytic cleavage, glycosylation, lipid modifications Proteins are usually modified after polymerization to give added functionality
Background image of page 6
Chemical rearrangement of amino acid residues occurs in the Green Fluorescent Protein
Background image of page 7

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

View Full DocumentRight Arrow Icon
Green Fluorescent Protein Reveals the Location of PIE-1 in C. elegans Roundworms
Background image of page 8
Predicting protein structure
Background image of page 9

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

View Full DocumentRight Arrow Icon
Summary for Chapter 2 Amino acids – know their names, structures and properties (please know the three letter and one letter abbreviations for future reading in Stryer) The peptide bond The disulfide bonds Protein structure – primary, secondary, tertiary and quaternary The α -helix and β -sheet Protein domains - folding and unfolding Disulfide bonds in the folding of Ribonuclease A (Anfinsen experiments Derivatives of amino acids
Background image of page 10
The NCBI is an exceptionally useful site PubMed site for searching literature Blast site for comparing protein and DNA sequences GenBank for Sequences of thousands of genomes PDB site for structures National Center for Bioinformatics http://www.ncbi.nlm.nih.gov/
Background image of page 11

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

View Full DocumentRight Arrow Icon
Stryer, Chapter 3 Outline: Proteins have different physical properties. These properties can be used to isolate populations of specific proteins from one another. The purified proteins can be characterized through
Background image of page 12
Image of page 13
This is the end of the preview. Sign up to access the rest of the document.

This note was uploaded on 01/16/2012 for the course BIOLCHEM 415 taught by Professor Michaeluhler during the Fall '06 term at University of Michigan.

Page1 / 53

Lecture 4 - Protein Purification - Biochem 415/515 -Lecture...

This preview shows document pages 1 - 13. Sign up to view the full document.

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