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The alpha helix is a secondary protein structure composed of hydrogen-bonded amino acids with spring-like properties. It plays a role in DNA and cellular cytoskeleton support, as well as the construction of hair, wool, and hooves. Polar charge contributes to stability, but if the structure breaks, it can disrupt cellular and biological functions. The effect of mechanical loading on these structures is not fully understood.
Protein is essential for life and comes in many forms. Their structure can vary, which can have a significant effect on amino acid functions and various biological functions. An alpha helix is composed of a chain of hydrogen-bonded amino acids, classifying the helix as a secondary protein structure. It is typically 10 amino acids long and has spring-like properties. Forces that can break bonds can damage a single helix as well as cell structure and deoxyribonucleic acid (DNA) binding.
If an alpha helix breaks, it can cause other local proteins to dissolve. Cellular functions and higher biological functions can be disrupted. Alpha helices store energy in their bonds, and it takes a force strong enough to break each bond for the structures to unravel their shape. They come in various patterns, such as helix-loop-helix motifs, and have a diameter equal to that of a groove in DNA.
The protein alpha helix serves as a structurally supporting component for DNA and cellular cytoskeletons on a larger scale. On larger biological dimensions, alpha helices are important in the construction of hair as well as wool and hooves. They also play a role in the composition of other structures, such as the alpha beta helix sheet, in which two or more chains of amino acids sit in parallel. There are multiple hydrogen bonds forming between the beta sheet strands to form a rigid structure. One side may be resistant to water molecules, while the other is charged and capable of interacting with or being altered by water.
Polar charge is a contributing factor to stability. An alpha helix is typically positively charged at one end and negatively charged at the other, which can destabilize the structure. A negatively charged amino acid is normally on the positive end, but sometimes a positively charged protein is on the negative end instead. Both arrangements stabilize the propeller and keep it intact.
Each alpha helix is submicroscopic but exhibits some degree of mechanical durability, even at the molecular level. Proteins are credited with a certain level of elasticity and strength, but the effect of mechanical loading on these structures is not fully understood. It is not known how deformation or failure occurs, but if cracking and unwinding occur, they can be harmful to the cells and biological functions of organisms.
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