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Molecular Interactions in Anatomy & Physiology

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  • What are the four major groups of biomolecules?

    Carbohydrates, lipids, proteins, and nucleotides are the four major groups of biomolecules.

  • What determines the element and isotope of an atom?

    Protons determine the element (atomic number), and neutrons determine the isotope of an atom.

  • What is the difference between isotopes and ions?

    Isotopes differ in neutrons, ions differ in electrons (gain or loss).

  • What are saturated, monounsaturated, and polyunsaturated fatty acids?

    Saturated fatty acids have no double bonds; monounsaturated have one double bond; polyunsaturated have two or more double bonds.

  • What is the backbone molecule of most lipids?

    Glycerol is a simple 3-carbon molecule that forms the backbone of most lipids.

  • What are phospholipids composed of?

    Two fatty acids and a phosphate group (–H2PO4).

  • What are eicosanoids and steroids?

    Eicosanoids are modified 20-carbon fatty acids acting as physiological regulators; steroids have four linked carbon rings and include cholesterol.

  • What are monosaccharides and their common types?

    Monosaccharides are simple sugars; common types include ribose (5-carbon) and glucose (6-carbon).

  • What are disaccharides and examples?

    Disaccharides consist of two monosaccharides; examples include sucrose, maltose, and lactose.

  • What are polysaccharides and their roles?

    Polysaccharides are glucose polymers used for energy storage or structure, e.g., glycogen, starch, cellulose, chitin.

  • What are the basic components of an amino acid?

    All amino acids have a carboxyl group (–COOH), an amino group (–NH2), a hydrogen, and a variable R group attached to the same carbon.

  • What is the primary structure of a protein?

    The sequence of amino acids in a peptide chain.

  • What types of bonds create secondary protein structure?

    Hydrogen bonds between adjacent chains or loops create alpha helices and beta sheets.

  • What is the quaternary structure of proteins?

    Multiple protein subunits combined by noncovalent bonds, e.g., hemoglobin.

  • What are nucleotides composed of?

    A phosphate group, a 5-carbon sugar (ribose or deoxyribose), and a nitrogenous base.

  • What is the difference between purines and pyrimidines?

    Purines have a double ring structure; pyrimidines have a single ring.

  • What are the main functions of single nucleotide molecules like ATP and NAD?

    They capture and transfer energy and aid in cell-to-cell communication.

  • What is the difference between covalent and noncovalent bonds?

    Covalent bonds share electron pairs and are strong; noncovalent bonds include ionic, hydrogen, and van der Waals forces and are weaker and reversible.

  • What is the role of hydrophilic and hydrophobic interactions in biological systems?

    Hydrophilic molecules dissolve in water due to polar or ionic regions; hydrophobic molecules repel water and tend to be nonpolar.

  • What is the induced-fit model of protein-ligand binding?

    The protein binding site changes shape to fit the ligand, allowing molecular complementarity.

  • What does the dissociation constant (Kd) indicate in protein binding?

    Kd indicates the affinity between protein and ligand; lower Kd means higher affinity.

  • What are cofactors and modulators in protein activity?

    Cofactors are required for active binding sites; modulators bind reversibly or irreversibly to alter protein activity.

  • How do temperature and pH affect protein function?

    Changes in temperature and pH can denature proteins, disrupting their structure and function.

  • What is the law of mass action in protein binding?

    At equilibrium, the ratio of bound to unbound protein and ligand remains constant.