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Amino Acid Sequence
The specific order of amino acids in a polypeptide chain that dictates a protein’s overall level of organization and final shape.
Protein Denaturation
Loss of a protein’s native three-dimensional structure, often caused by changes in temperature or pH, resulting in loss of function.
Temperature (Protein Stability)
A physical factor that can disrupt weak bonds within proteins, contributing to changes in structure or denaturation.
pH (Protein Stability)
A measure of hydrogen-ion concentration; extreme values can disrupt ionic and hydrogen bonds in proteins and alter their structure.
Secondary Structure (Protein)
Local folding of a polypeptide into α-helices or β-sheets, stabilized primarily by hydrogen bonds.
Hydrogen Bond
A weak attraction between a slightly positive hydrogen and a slightly negative atom (such as O or N) that stabilizes protein secondary structure.
Adenosine Triphosphate (ATP)
The cell’s primary energy currency, consisting of adenine, ribose, and three phosphate groups; hydrolysis of its terminal phosphate releases energy.
Adenosine Diphosphate (ADP)
The molecule produced when ATP loses its terminal phosphate group along with the release of usable energy.
High-Energy Phosphate Bond
The unstable covalent linkage between phosphate groups in ATP that stores significant chemical energy.
Dehydration Synthesis
An anabolic reaction that links monomers to form polymers by removing a molecule of water.
Hydrolysis
A catabolic reaction that breaks polymers into monomers by adding a molecule of water.
Phospholipid
A lipid composed of glycerol, two fatty acids, and a phosphate group; forms the structural basis of cell membranes.
pH Scale
A logarithmic scale ranging from 0 to 14 that indicates the acidity or alkalinity of a solution; each unit represents a ten-fold change in H+ (or OH−) concentration.
Buffer
A chemical system that resists drastic changes in pH by absorbing or releasing hydrogen (H+) or hydroxide (OH−) ions.