B2.1

Cards (36)

  • Passive Transport
    Passive transport involves the movement of material along a concentration gradient (high concentration ⇒ low concentration)
    • Because materials are moving down a concentration gradient, it does not require the expenditure of energy (ATP hydrolysis)
  • what are the three main types of passive transport:
    • Simple diffusion – movement of small or lipophilic molecules that can freely cross the bilayer
    • Osmosis – movement of water molecules across the bilayer (dependent on solute concentrations)
    • Facilitated diffusion – movement of large or charged molecules via transmembrane proteins
  • Active Transport
    Active transport involves the movement of materials against a concentration gradient (low concentration ⇒ high concentration)
    • Because materials are moving against the gradient, it does require the expenditure of energy (ATP hydrolysis)
  • what are two main types of active transport:
    • Primary active transport – A molecule is moved against its gradient using energy from the hydrolysis of ATP
    • Secondary active transport – A molecule is moved against its gradient coupled to another molecule moving  down an electrochemical gradient (cotransport)
  • The rate of diffusion can be influenced by a number of factors, including:
    • Temperature (affects kinetic energy of particles in solution)
    • Molecular size (larger particles are subjected to greater resistance within a fluid medium)
    • Steepness of gradient (rate of diffusion will be greater with a higher concentration gradient)
  • what is this
    the generalized structure of an amino acid.
  • Define Protiens
    complex macromolecules composed of one or more chains of amino acids.
  • Proteins play an important role in many biological processes including, ..
    • structural support, catalysis and signalling pathways.
  • Define Amino acids
    the monomers that are used to make proteins.
  • How many type of amino acids are there
    20
  • Amino acids join together through a condensation reaction. 
    • A peptide bond is formed when the carboxyl group (-COOH) of one amino acid reacts with the amino group (-NH2) of another amino acid to form a dipeptide.
    • A water (H2O) molecule is released as a by product. 
    • The peptide bond formed is a type of covalent bond and therefore is very stable. 
  • The structure of an amino acid contains
    • Amine Group (NH2)
    • Carboxyl group (COOH
    • Alpha Carbon (c)
    • R Group
  • Amino acid structure - Amine Group (NH2):
    • the -NH2 group attached to the alpha carbon 
  • amino acid structure - Carboxyl group (COOH)
    • The -COOH group attached to the alpha carbon 
  • Amino acid structure - Alpha Carbon (c)
    •  the central carbon to which the amine group, carboxyl group, hydrogen atom and R groups are attached. 
  • amino acid structure - R Group:
    • the side chain that varies between different amino acids. 
  • what makes every type of amino acid different
    The R group
  • Amine Group
    NH2
  • Carboxyl group
    COOH
  • alpha carbon
    C
  • R group
    R
  • Condensation reaction between two amino acids. Once the water is removed, ...

    the C bonds to the N in a peptide bond.
  • Dipeptide
    a molecule consisting of two amino acids joined by a single peptide bond. 
  • Oligopeptide
    a molecule composed of a few (typically 2-20) amino acids. 
  • Polypeptide
    a longer chain of amino acids, typically longer than 20 residues, but not yet a fullt functional protein
  • Longer polypeptide chains
    Formed by adding amino acids through peptide bonds
    1. terminal (amino-terminal) end
    Refers to the free amino group not involved in the peptide bond
    1. terminal (carboxyl-terminal) end
    Refers to the unbound carboxyl group
  • Formation of longer polypeptide chains
    1. Add amino acids to dipeptide
    2. Form new peptide bond
    3. Repeat process multiple times
  • Each time an amino acid joins the growing polypeptide strand

    A new peptide bond is formed and a water molecule is released
  • More amino acids can be added to the dipeptide by forming a new peptide bond between an incoming amino acid and the C-terminal of the dipeptide
  • This process can be repeated multiple times to form longer chains of amino acids, called polypeptides
  • Location of polypeptide formation 
    • Polypeptide formation occurs in the ribosome of a cell, which can be found in the cytoplasm or on the rough endoplasmic reticulum.
  • Source of amino acids:
    • Plant cells 
    • Animal cells
  • Amino acids can be essential or non-essential
    • Essential amino acids = are the amino acids that your body cannot produce and therefore you must obtain them from the food that you eat. 
    • Necessary for proper growth, maintenance and repair of the body’s tissues and organs
    • non-essential amino acids = can be produced by the body from other amino acids or by the breakdown of proteins. 
    • It is important to have but not required
  • Source of amino acids:
    • Plant cells: produce amino acids through photosynthesis and other metabolic processes
    • Animal cells: obtain amino acids through the consumption of food