Transcript Tennis Racquet Strings

Tennis Racquet Strings
(Natural Gut)
How It Is Made
Natural gut’s main source is a cow intestine called serosa. It is long and has
great tensile strength. The collagen found in serosa has a molecular make up
that is designed to withstand the stretching and contraction of the intestine.
It takes three cows to produce one set of tennis string. To produce this string
is a very long, involved process. Once the serosa is removed from the cow, it is
cut into long ribbons, which go through a long cleaning process afterward.
Although it varies depending on the manufacturer, the ribbons are most of
the time put into a variety of baths. The purpose of this is to remove
impurities without harming anything. Sometimes, the string is bleached to
remove the orange color of the ribbons.
http://www.tennis-warehouse.com/lc/Naturalgut.html
How It Is Made
Once the ribbons have been washed, they are subjected to more
quality control. The manufacturer may add some color to the
string. The ribbons are then bound together on tension racks and
the drying process begins. This process is carefully controlled
down to the climate. It might even take several days. Once
bound together they will finally start to look like string. It needs
to be polished for smoothness and checked to make sure it
meets the correct gauge specifications. At this point, most
manufacturers will coat the string with a special polyurethane
coating to improve abrasion and water resistance. The string is
finally prepared for packaging.
http://www.tenniswarehouse.com/lc/Naturalgut.html
Composition
Collagen has a triple helix molecular structure. It is made of
three polypeptide strands stabilized by numerous hydrogen
bonds. It is the single most abundant protein in the animal
kingdom. Collagen’s structural unit is 300-nm long and 1.5-nm in
diameter. It consists of three coiled subunits: two α1(I) chains
and one α2(I).* Each chain contains 1050 amino acids.
The triple-helical structure arises from an abundance of three
amino acids, which include glycine, proline, and hydroxyproline.
Hydrogen bonds linking the peptide bond NH of a glycine residue
with a peptide carbonyl (C═O) group in an adjacent polypeptide
help hold the three chains together. The fixed angle of the C – N
peptidyl-proline or peptidyl-hydroxyproline bond enables each
polypeptide chain to fold into a helix
http://www.ncbi.nlm.nih.gov/books/NBK21582/
http://liamscheff.com/wp-content/uploads/2010/02/collagenmolecule-fibril.jpg
http://web.mit.edu/course/3/3.082/www/team1_f02/pictures/collag
enstructure.jpg
LEWIS DOT STRUCTURE
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