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Protein Structure

©2001 Timothy Paustian, University of Wisconsin-Madison

General Function

Proteins and peptides (small proteins) are essential to the cell. They serve two major functions in the cell. Some proteins are enzymes that catalyze most biological reactions in a living organism. Other proteins perform a structural role for the cell - either in the cell wall, the cell membrane or in the cytoplasm. In this section, we will look at the basic structure that all proteins have in common.

Primary Stucture

Protiens are polymers of amino acids. Amino acids are primary amines that contain an alpha carbon that is connected to an amino (NH3) group, a carboxyl group (COOH), and a variable side group (R) - see Figure 1. The side group gives each amino acid its distinctive properties and helps to dictate the folding of the protein.

The basic structure of an amino acid

Figure 1 - A general amino acid.

Polymers of amino acids are created by linking an amino group to a caroboxyl group on another amino acid. This is termed a peptide bond - Figure 2.

PeptideBond.JPG

Figure 2 - A peptide bond

There are 20 common amino acids found in proteins and these amino acids can be classified into 3 groups; polar, non-polar and charged. Polar and charged amino acids will most often be found on the surface of a protein, interacting with the surrounding water, while the non-polar (or hydrophobic) amino acids will bury themselves in the interior. The number and position of these types of amino acids in protein can greatly influence its function. Figure 3 shows the chemical structure of the amino acids.

aminoacids.JPG

Figure 3 - The common amino acids

Peptides and proteins are formed when a ribosome and the rest of the translation machinery link 10 - 10,000 amino acids together in a long polymer. This long chain is termed the primary sequence. The properties of the protein are determined, for the most part, by this primary sequence. In many cases an alteration of any amino acid in the sequence will result in a loss of function for the protein (a mutation). Genetic diseases in humans are often caused by changes in important proteins that causes illness. Sickle cell anemia is caused by a single amino acid change from glutamic acid to valine at position 6 of the hemoglobin protein. Below is the primary sequence of hemoglobin, the oxygen carrying protein found in humans and other mammals.

HemoglobinPrimary.GIF

Figure 4 - Hemoglobin amino acid sequence. Only the first 26 amino acids are shown.

Secondary Structure

Basic attractive forces

During and after synthesis, the primary sequence will associate in a fashion that leads to the most stable, "comfortable" structure for the protein. How a protein folds is largely dictated by the primary sequence of amino acids. Each amino acid in the sequence will associate with other amino acids to conserve the most energy. This structure is stabilized by hydrogen bonds, hydrophobic interactions, ionic interactions, and sulfhydryl linkages. We have covered the first three in Chapter 2, but sulfhydryl linkages need to be introduced.

Sulfhydryl linkages. These are covalent bonds between cysteine groups. Cysteine is a unique amino acid in that it has a sulfur group available for binding to other groups. Often in proteins, adjacent sulfhydryl groups on cysteines will form a covalent link in a protein - Figure 5 and are often crucial for the mature protein to perfom its function.

CystStructure.JPGCystsequence.JPG
The chemical structure of a sulhydryl bondA sulfhydryl bond in a peptide

Figure 5 - Two views of sulfhydryl linkages

Common Secondary Structures

Proteins will often have stretches of amino acids that will associate into two common structures. These are the alpha helix and the beta (pleated) sheet. Formation of these structures is driven by favorable hydrogen bonding and hydrophobic interactions between nearby amino acids in the protein.

The alpha helix resembles a ribbon of amino acids wrapped around a tube to form a stair case like structure. Below is pictured a ribbon and ball and stick diagram of a model alpha helix. This structure is very stable, yet flexible and is often seen in parts of a protein that may need to bend or move.

AlphaRibbon.JPG
Ribbon
Alpha.JPG
Ball and stick

Figure 6 - The alpha helix

In the beta sheet, two planes of amino acids will form, lining up in such a fashion so that hydrogen bonds can form between facing amino acids in each sheet. The beta pleated sheet or beta sheet is different than the alpha helix in that far distant amino acids in the protein can come togeher to form this structure. Also, the structure tends to be rigid and less flexible.

bsheetribbontop.JPG
Ribbon top view
BSheetRibbon.JPG
Ribbon side view
BetaSheetsideview.JPG
Ball and stick side view

Figure 7 - The beta sheet

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