Hi, I'd like some explanations of what the primary, secondary, and tertiary structures of proteins, protein purification, and basic protein spectroscopy are. I've taken only 2 quarters of inorganic chemistry. Most of my work has been in stoichiometry. Anybody think they can give me an explanation of these things?

somebody must know. But he tell me whats up with this--- the idea of enzyme and substrate bonding is just a theory-- the old theory was lock and key, the new theory is induced fit. so we don't know for certain how they work, and yet we use restriction endonucleases (which are enzymes right?) to genetically engineer? Pretty amazing.

As far as I remember, the primary structure of a protein refers to the order of amino acids in the peptide chain (unique to each protein). The secondary structure refers to the conformation of the protein in space; Alpha helix, Beta-pleated sheet and so-on. The tertiary structure refers to the conformation of a protein in relation to those around it in a functional unit, as in for example the four-unit globin complex in haemoglobin.

 

As for your other questions, I'm afraid I don't know.

Yeah, primary structure is the sequence of amino acids in polypeptide. But secondary structure is simply the helices and sheets, and tertiary is how these are arranged in space, along with the connecting loops of the peptide. Where multiple polypeptides form a protein (as in haemoglobin) this is called the quaternary structure.

 

scm007, you're best off looking on google for sites that explain these things.

Oh yeah...I had a feeling I missed one somewhere.

De nada, I don't think they needed to know quaternary anyway.