For pinkfreud....My 10 yr. old grandson is in a summer enrichment
program in Georgia and his project is to find out how alcohol kills
germs.  Can you or someone try this one.  Thanks

"Ethyl alcohol kills germs by denaturing their protein, which means
that germs cannot "mutate" or suddenly become resistant to ethyl
alcohol and not be killed by it.  Ethyl alcohol has been used to kill
germs for centuries now, and no organisms are known to be resistant to
it."

Thatcher Pharmaceutical
http://tpharm.tchem.com/gelsan/consumer.htm

"The antimicrobial activity of alcohols can be attributed to their
ability to denature proteins (120). Alcohol solutions containing
60%--95% alcohol are most effective, and higher concentrations are
less potent (120--122) because proteins are not denatured easily in
the absence of water (120)."

"Guideline for Hand Hygiene in Health-Care Settings" Prepared by 
John M. Boyce, M.D. and Didier Pittet, M.D. Center for Disease Control
http://www.cdc.gov/mmwr/preview/mmwrhtml/rr5116a1.htm

Having discovered that alcohol solutions' ability to act as an
antiseptic is because of their ability to denature proteins, I then
located the following resource explaining denaturation of proteins,
along with the specific process employed by alcohol solutions:

"Denaturation of proteins involves the disruption and possible
destruction of both the secondary and tertiary structures. Since
denaturation reactions are not strong enough to break the peptide
bonds, the primary structure (sequence of amino acids) remains the
same after a denaturation process. Denaturation disrupts the normal
alpha-helix and beta sheets in a protein and uncoils it into a random
shape.

Denaturation occurs because the bonding interactions responsible for
the secondary structure (hydrogen bonds to amides) and tertiary
structure are disrupted. In tertiary structure there are four types of
bonding interactions between "side chains" including: hydrogen
bonding, salt bridges, disulfide bonds, and non-polar hydrophobic
interactions. which may be disrupted. Therefore, a variety of reagents
and conditions can cause denaturation. The most common observation in
the denaturation process is the precipitation or coagulation of the
protein."

"Alcohol Disrupts Hydrogen Bonding:

Hydrogen bonding occurs between amide groups in the secondary protein
structure. Hydrogen bonding between "side chains" occurs in tertiary
protein structure in a variety of amino acid combinations. All of
these are disrupted by the addition of another alcohol.

A 70% alcohol solution is used as a disinfectant on the skin. This
concentration of alcohol is able to penetrate the bacterial cell wall
and denature the proteins and enzymes inside of the cell. A 95%
alcohol solution merely coagulates the protein on the outside of the
cell wall and prevents any alcohol from entering the cell. Alcohol
denatures proteins by disrupting the side chain intramolecular
hydrogen bonding. New hydrogen bonds are formed instead between the
new alcohol molecule and the protein side chains."

http://www.elmhurst.edu/~chm/vchembook/568denaturation.html
"Denaturation of Proteins" Virtual Chembook by Charles E. Ophardt,
Elmhurst College, 2003

I hope you found the above resources helpful.

Sincerely,

Wonko

wonko,

Since the customer specifically requested me by name, I do wish you'd
allowed me the opportunity to answer this interesting question.

Best regards,
pinkfreud

Wonko-ga,

I am amazed by your lack of good behavior.

Scriptor

Hi Wonko,

You might want to peruse the newsletter archive when you have a few
moments, and brush up on the policy of leaving questions specifically
directed at other Researchers alone.  Please do right by our
customers, and honor their wishes when they request a specific
Researcher.

Perhaps you didn't realize that the customer asked for Pinkfreud when
you first read this question.  You should consider doublechecking all
questions before proceeding - it's easy to miss this little detail if
you're answering on the fly.

--Missy