biochem

    Cards (86)

    • What are the three main macromolecules in biochemistry?
      Proteins, lipids, nucleic acids
    • Why are enzymes important in biochemistry?
      They act as biological catalysts and drug targets
    • What does biochemistry study?
      Atoms and molecules in living organisms
    • How does biochemistry bridge biology and chemistry?
      By explaining molecular mechanisms of life processes
    • What are biological macromolecules?
      Structures that provide cell structure and functions
    • How does biochemistry help in medicine?
      Advancements in drug development and diagnostics
    • What elements are essential for life?
      Carbon, Hydrogen, Oxygen, Nitrogen, Phosphorus, Sulphur
    • How many chemical elements occur naturally in plants and animals?
      About 31 elements
    • What percentage of the dry weight of living things is made up of C, H, O, N, P, and S?
      About 92%
    • What are trace elements in biological material?
      Elements in small quantities essential for life
    • What is the zwitterion form of amino acids?
      Amino acids with both positive and negative charges
    • What happens to the carboxylic acid group in zwitterions?
      It donates a proton to the amino group
    • How are amino acids esterified?
      By heating with alcohol and sulfuric acid
    • What is the result of acylation of the amino group?
      Conversion to an amide with acylating agents
    • What occurs when amino acids react with strong acids?
      They behave as bases and form positive ions
    • What occurs when amino acids react with strong alkalis?
      They behave as acids and form negative ions
    • What color indicates the presence of amino acids in the Ninhydrin test?
      Purple
    • What is a protein?
      A biological polymer made of amino acids
    • What are the functions of proteins?
      Structure, catalysis, movement, transport, hormones
    • How many different amino acids are used to build proteins?
      Twenty different amino acids
    • What is a peptide bond?
      A bond linking two amino acids together
    • What is the N-terminus of a peptide chain?
      The end with the amine group (NH2)
    • How is the amino acid sequence of a peptide displayed?
      Amino terminal end on the left, carboxyl on the right
    • What defines primary protein structure?
      Covalent peptide bonds forming a polypeptide chain
    • What can mutations in the amino acid sequence affect?
      Protein folding and function
    • What is secondary protein structure characterized by?
      Hydrogen bonding between peptide bonds
    • How is an α-helix formed?
      By hydrogen bonding between peptide bonds
    • What characterizes a β-pleated sheet?
      Hydrogen bonds between amino acids on different sheets
    • What is tertiary protein structure?
      Folding of the polypeptide chain into 3D shape
    • What can disrupt tertiary protein structure?
      Disruption of bonds between R groups
    • What is protein denaturation?
      Loss of protein shape and function
    • What types of bonds are involved in tertiary protein structure?
      Hydrogen, electrostatic, covalent, hydrophobic bonds
    • What is quaternary protein structure?
      Linking of multiple polypeptide chains
    • What is the role of fully functional proteins?
      Perform specific roles within the body
    • What is an enzyme?
      A protein that catalyzes biological reactions
    • How do enzymes affect activation energy?
      They lower the activation energy of reactions
    • What factors affect enzyme activity?
      pH, enzyme concentration, substrate concentration, temperature
    • What is enzyme-substrate specificity?
      Enzymes bind specifically to their substrates
    • What is the active site of an enzyme?
      A specific region that binds to the substrate
    • What happens to the substrate in the presence of an enzyme?
      It is modified to produce a product
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