CHEM 440
Biochemistry I

J. D. Cronk   Syllabus [ Previous | Next ] Pick a lecture:
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Lecture 9. Protein methods

Wednesday 23 September 2009

More peptide and protein methods. Peptide and protein sequencing methods. Mass spectrometry of proteins.

Reading: BTS6 - Ch.3, pp.78-84


9. Protein stability and folding

Lecture 9 Summary

Update for Fall 2009 in progress...

We will cover at least some of the following topics, for the most part also found in Ch.3, BTS6.

Protein sequencing. Mass spectrometry of proteins and peptides.

Techniques for chemical and enzymatic cleavage of proteins

Chemical cleavage: Cyanogen bromide (CNBr) cleaves after Met residues; hydroxylamine cleaves Asn-Gly bonds.

Enzymatic cleavage: Relies on proteases with well-defined specificities. Examples: trypsin (after Arg, Lys residues), clostripain (after Arg residues), thrombin, chymotrypsin, carboxypeptidase A.

Structure determination: Tertiary and higher structures are obtained experimentally by X-ray crystallography and multidimensional nuclear magnetic resonance (NMR).

 

 

 

Learning objectives

Page update in progress

References

 
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[ E-mail: cronk@gonzaga.edu ]