BIOCHEMISTRY WEBSITE

http://www.wiley.com/college/boyer/0470003790/animations/translation/translation.htm

This is the perfect interactive website tool to replicate the synthesis of proteins. Although this particular slide is on the proteins involved in just the transcription and translation processes, there are a wide variety of animations available to watch but simply returning one webpage closer to wiley.com and then there will be a list of all animations available.      

       In addition to this website, there are numerous other interactive biochemistry webpages which I came across by typing in the key word animation. Being somewhat of a visual learner, I find these to be extremely helpful!

KNOWLEDGE CONNECTED WITH PAST KNOWLEDGE

I have had a great deal of previous learning experience dealing with both enzymes and hormones and proteins which function as enzymes. Now that we are involved in discussing this topic, I have found the lecture material to be a reminder of the importance of the many different functions that a protein can have in the body. Our discussion on subunits and the folding of a protein structure is both a connection with past knowledge I have as well as one of what I find to be the most interesting aspects of our biochemistry class so far. I can recall having been introduced to this material but the identification of which amino acids are part of which structures, as well as the action of enzymes on protein structure to either catalyze a reaction or alter it in some way, are new aspects of protein identification to me. I truly do find protein structure and synthesis to be an interesting topic to cover and one that is relative to our everyday lives on many levels!

PROTEIN USING PDB EXPLORER

 

Alcohol Dehydrogenase, or aldehyde reductase, is found in a wide variety of species (even those which don’t consume alcohol!) because the primary purpose of a dehydrogenase enzyme is to utilize a mechanism to convert alcohol into aldehydes or ketones. ADH can not only oxidize ethanol to acetaldehyde (as most college students can relate to) but they can also oxidize secondary, cyclic secondary, or hemi-acetal  alcohols.

                Each of the subunits on ADH has two different domains; an NAD binding domain which is shown in purple and green, and also an alcohol (substrate) binding domain which is shown in blue and yellow. These two subunits with their respective domains makes ADH active as a dimer in humans.

                Another note about structure is that ADH uses two molecules to act as tools and help it perform a reaction on ethanol when ingested. A zinc atom is used to hold and position the alcohol group on ethanol. The other tool utilized is a large NAD cofactor which is the work-horse and actually performs the reaction. The mechanism to describe how this works can be found here:

http://www.users.csbsju.edu/~hjakubow/classes/rasmolchime/99ch331proj/alcoholdehydro/mech.htm

Works Cited:

Alcohol Dehydrogenase.  20 May, 1999. Retrieved from    http://www.users.csbsju.edu/~hjakubow/classes/rasmolchime/99ch331proj/alcoholdehydro/index.htm. Feb 27, 2011.

Goodsell, D. (2001, December). Alcohol Dehydrogenase. Retrieved from http://www.rcsb.org/pdb/101/motm.do?momID=13