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3.4 Proteins -- Part 2
A coiling and a b sheet were the two basic patterns of structure that were found in the structure of the amino acids.
They discovered that the a helix was the first and the b sheet was the second.
Each polypeptide can have multiple sheets.
B sheets are formed when the polypeptide turns back onto itself, allowing hydrogen bonding to occur between the extended lengths of the polypeptide.
Silk, a silk that forms spider webs, is an example.
The primary structure of both of these proteins is shown in Figure 3.17.
Structural proteins are fronus.
For example, in hair, horns, and hooves, it's possible to find kerat.
A perm is a chemical treatment that can be used to alter the secondary structure of a proteins.
Silk is made by spiders and is made into pleats.
The sheet is double back on itself because of hydrogen bonding between parts of the molecule.
The interaction of the water with the polypeptide chain is a major factor in how the final shape of the molecule is created.
To be as far away from water as possible, these nonpolar amino acids are grouped together in the interior of a protein.
The polar hydrophilic and ionic amino acids tend to orient themselves on theProtein's surface when interacting with water.
The tertiary shape can be maintained with strong disulfide linkages.
The majority of the enzymes are made of the same type of proteins.
The rate of the reaction is the highest when the pH is optimal.
The normal shape of the enzyme can be maintained at this temperature and pH.
The shape of the enzyme can be disrupted by a high temperature and change in pH.
Denatured is the term used to describe the loss of the natural shape of a proteins.
An organisms metabolism can no longer be maintained if too many genes are denatured.
There are four polypeptides in hemoglobin, the molecule that transports oxygen in the blood.
The primary, secondary, and tertiary structure of the polypeptide are found in hemoglobin.
There are only two polypeptides and quaternary structure in a protein.
The function of a molecule is related to its structure.
The correct folding of aProtein is important.
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