1. Proteins
Primary structure: Amino acids link together to form a linear polypeptide.
The primary structure of a protein is a linear chain of amino acids.
An amino acid monomer is composed of a central carbon atom, called the alpha (α) carbon.
An alpha carbon in a protein bonds to (1) an amino group, (2) a side chain or R-group, (3) a carboxyl group, and (4) a hydrogen atom.
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2. Figure 1 Amino acid structure.
Proteins
Figure 1 Amino acid structure.
An amino acid contains an amino group, a side chain, a carboxyl group, and a hydrogen atom all bound to a central carbon atom.
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3. Proteins Figure 2 The 20 amino acids.
The amino group and the carboxyl group are always the same, but the R-group differs in each of the 20 amino acids. The side chain determines whether the amino acid will be polar, nonpolar, or electrically charged.
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4. Proteins
Primary structure: Amino acids link together to form a linear polypeptide.
Amino acids combine in different orders, which changes the electronegativities of the molecules and how different parts of the chain bind together to form tertiary and quaternary levels of structure.
Mathematically, the 20 amino acids can combine to form millions of different proteins in chains of varying length.
A carboxyl group can bond to an amino group by a dehydration reaction-the removal of a water molecule. This reaction forms a peptide bond. Dehydration reactions link amino acids into polypeptide chains. A polypeptide backbone forms from a chain of alpha carbons, which are carboxyl and amino groups linked by peptide bonds, excluding the R-groups. Peptide bonds are the chemical bonds of carbon to nitrogen after dehydration. Side groups, as their name suggests, stick out to the sides of the backbone. Polypeptide chains range in length from a few amino acids to more than a thousand.
A carboxyl group can bond to an amino group by a dehydration reaction-the removal of a water molecule-thereby forming a peptide bond.
Peptide bonds are the chemical bonds of carbon to nitrogen after dehydration.
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5. Proteins Figure 3 Peptide bond.
A peptide bond is formed between the carboxyl and amino groups of adjacent amino acids.
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6. Proteins
Secondary structure: Hydrogen bonds between atoms in the polypeptide backbone create a folded or coiled shape.
Segments of the polypeptide chain can form coiled or folded patterns, called the secondary structure.
A polypeptide backbone forms from a chain of alpha carbons, which are carboxyl and amino groups linked by peptide bonds, excluding the R-groups.
Looping coils (α helices) develop from the hydrogen bonds that form between the oxygen of a carboxyl group and the hydrogen of the fourth amino group in the chain.
Folded patterns (β pleated sheets) form when two or more strands of a polypeptide line up parallel to one another. Hydrogen bonds form between adjacent carboxyl and amino groups.
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7. Figure 4 Secondary structures.
Proteins
Figure 4 Secondary structures.
Hydrogen bonds between amino and carboxyl groups hold together structures such as α helices and β pleated sheets. In ribbon diagrams, the flat arrow points to the carboxyl end of the polypeptide.
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8. Proteins
Tertiary structure: Interactions between side chains create a three-dimensional shape.
Tertiary structure is the main, three-dimensional shape of a polypeptide unit.
Tertiary structure results from, and is held together by, bonds and interactions between R-groups and between R-groups and elements on the backbone.
• The hydrophobic effect is the clustering of nonpolar side chains or burial of the core of the protein molecule in a manner that reduces contact with water molecules in the surrounding fluid. • Covalent bonding affects tertiary structure. Two sulfur atoms can bond together covalently, often called disulfide bridges. • Hydrogen bonding, ionic bonding, and van der Waal interactions can affect tertiary structure.
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9. Proteins
Quaternary structure: Associations of polypeptides form a functional protein.
Quaternary structures result from the aggregation of the tertiary structures that may be the same subunits or different subunits.
Quaternary structures use the same palette of bonds and interactions used to form tertiary structures, only the bonds and interactions occur between atoms of separate polypeptide units.
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10. Proteins Figure 7 Collagen.
Collagen’s molecular structure is ideal for resisting pulling strain. Its three polypeptide chains are twisted together like the strands of a rope. Analysis of collagen’s lower structural levels reveal that this folding pattern is further stabilized by hydrogen bonding among the three polypeptide chains.
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11. Figure 8 Structure of the glutamate receptor.
Proteins
Figure 8 Structure of the glutamate receptor.
A glutamate receptor is composed of four subunits, each shown here in a different color. The subunits form prong-like shapes similar to the top of the capital letter Y. Binding of the neurotransmitter glutamate to the glutamate receptor at the prongs of the Y modifies the receptor’s structure and causes the ion channel at the bottom of the glutamate receptor to open (at the stem of the “Y”; opening not shown). The stem of the Y is the area of the receptor embedded in the cell membrane.
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12. Proteins
BIOSKILL
X-ray Crystallography is an Important Technique in Determining Protein Structure
Scientists use x-ray crystallography-a technique that measures the angle and intensity with which x-rays are diffracted when passing through a crystalline structure-to determine the structures of many biological molecules.
Most famously, Rosalind Franklin ( ) used x-ray crystallography in the discovery of DNA's double helix.
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13. Figure 9 X-ray diffraction.
Proteins
Figure 9 X-ray diffraction.
Rosalind Franklin showed DNA’s helical structure with x-ray diffraction in This process and image became the foundation for establishing the shape of many other biological molecules including proteins.
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14. Proteins
Figure 10 Comparing electron density maps with three-dimensional ribbon models.
Pay attention to the locations of the structures on the electron map marked by researchers and where these locations correspond to the model. Scientists interpret the electron density map to identify the locations of amino acids such as Ala 753 as seen in panel a to get the structure of and position of the same part of the protein in panel b.
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15. Future perspectives. Proteins Principles of Biology
In the 1990s, research confirmed the existence of strange infectious proteins called prions, which lack genetic material.
Prions cause fatal neurodegenerative diseases such as bovine spongiform encephalopathy (BSE, or "mad cow" disease) and Creutzfeldt-Jakob disease (CJD).
In BSE and CJD, normal cellular prion protein (PrPC), which is naturally occurring in the brain, is converted structurally into the infectious prion protein PrPSc through a process that increases its beta-sheet content.
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