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In this module: |
| Introduction |
| Amino Acids |
| Hydrophobic and Polar Amino Acids |
| Acidic and Basic Amino Acids |
| Peptide Bonds |
| Planarity of Peptide Bonds |
| Protein Sequences |
| Sickle Cell Anemia |
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Amino acids are grouped according to what their side chains are like. The nine amino acids that have hydrophobic | |
Polar Amino Acids | |
Six amino acids have side chains that are polar | |
The building blocks of proteins are amino acids, which are small organic molecules that consist of an alpha (central) carbon atom linked to an amino group, a carboxyl group, a hydrogen atom, and a variable component called a side chain (see below). Within a protein, multiple amino acids are linked together by peptide bonds, thereby forming a long chain. Peptide bonds are formed by a biochemical reaction that extracts a water molecule as it joins the amino group of one amino acid to the carboxyl group of a neighboring amino acid. The linear sequence of amino acids within a protein is considered the primary structure of the protein.
Proteins are built from a set of only twenty amino acids, each of which has a unique side chain. The side chains of amino acids have different chemistries. The largest group of amino acids have nonpolar side chains. Several other amino acids have side chains with positive or negative charges, while others have polar but uncharged side chains. The chemistry of amino acid side chains is critical to protein structure because these side chains can bond with one another to hold a length of protein in a certain shape or conformation. Charged amino acid side chains can form ionic bonds, and polar amino acids are capable of forming hydrogen bonds. Hydrophobic side chains interact with each other via weak van der Waals interactions. The vast majority of bonds formed by these side chains are noncovalent. In fact, cysteines are the only amino acids capable of forming covalent bonds, which they do with their particular side chains. Because of side chain interactions, the sequence and location of amino acids in a particular protein guides where the bends and folds occur in that protein (Figure 1).
Figure 1: The relationship between amino acid side chains and protein conformation
The defining feature of an amino acid is its side chain (at top, blue circle; below, all colored circles). When connected together by a series of peptide bonds, amino acids form a polypeptide, another word for protein. The polypeptide will then fold into a specific conformation depending on the interactions (dashed lines) between its amino acid side chains.
Figure 2: The structure of the protein bacteriorhodopsin
Bacteriorhodopsin is a membrane protein in bacteria that acts as a proton pump. Its conformation is essential to its function. The overall structure of the protein includes both alpha helices (green) and beta sheets (red).
The primary structure of a protein — its amino acid sequence — drives the folding and intramolecular bonding of the linear amino acid chain, which ultimately determines the protein's unique three-dimensional shape. Hydrogen bonding between amino groups and carboxyl groups in neighboring regions of the protein chain sometimes causes certain patterns of folding to occur. Known as alpha helices and beta sheets, these stable folding patterns make up the secondary structure of a protein. Most proteins contain multiple helices and sheets, in addition to other less common patterns (Figure 2). The ensemble of formations and folds in a single linear chain of amino acids — sometimes called a polypeptide — constitutes the tertiary structure of a protein. Finally, the quaternary structure of a protein refers to those macromolecules with multiple polypeptide chains or subunits.
The final shape adopted by a newly synthesized protein is typically the most energetically favorable one. As proteins fold, they test a variety of conformations before reaching their final form, which is unique and compact. Folded proteins are stabilized by thousands of noncovalent bonds between amino acids. In addition, chemical forces between a protein and its immediate environment contribute to protein shape and stability. For example, the proteins that are dissolved in the cell cytoplasm have hydrophilic (water-loving) chemical groups on their surfaces, whereas their hydrophobic (water-averse) elements tend to be tucked inside. In contrast, the proteins that are inserted into the cell membranes display some hydrophobic chemical groups on their surface, specifically in those regions where the protein surface is exposed to membrane lipids. It is important to note, however, that fully folded proteins are not frozen into shape. Rather, the atoms within these proteins remain capable of making small movements.
Even though proteins are considered macromolecules, they are too small to visualize, even with a microscope. So, scientists must use indirect methods to figure out what they look like and how they are folded. The most common method used to study protein structures is X-ray crystallography. With this method, solid crystals of purified protein are placed in an X-ray beam, and the pattern of deflected X rays is used to predict the positions of the thousands of atoms within the protein crystal.