Protein shape part one

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  1. Proteins are therefore (because they have peptide bonds that hop the long chain of amino acids, are called___________. In each type of protein, the amino acids are present in a unique order, called the _____________, which is exactly the same from one molecule of that protein to the next.

    Each polypeptide chain consists of a backbone that is adorned with a variety of chemical side chains called __________, formed from a repeating sequence of the core atoms found in every amino acid.

    Projecting from the polypeptide backbone are the amino acid ________.

    Amino acid sequences

    Polypeptide backbone

    Side chain.
  2. Why are the long polypeptide chains very flexible and in principle are able to fold in an enormous number of ways?

    What hat constrains the shape of each of the folded chains?

    What are the non covalent bonds that help proteins fold up and maintain their shape?

    What is the fourth weak force?
    Because the peptide bonds that link the carbon atoms in the polypeptide backbone allow free rotation of the atoms they join.

    Noncovalent bonds that form within the proteins

    Hydrogen bonds, electrostatic bonds, and Van der Waals forces.

    Hydrophobic Force.
  3. What is an important factor in the folding of proteins?

    Where to the non polar amino acids tend to aggregate or cluster in? Why?

    Where do the polar amino acids tend to arrange them selves?

    What happens when polar amino acids are located in interior of the folded protein?

    What type of forces specifically help proteins fold into compact conformations?
    The distribution of its polar and non polar amino acids.

    The interior of the folded protein because there they tend to avoid the aqueous environment of the cytosol that surrounds them inside the cell.

    To the outside of the folded protein.

    They tend to hydrogen bond to each other or to the polypeptide backbone.

    Hydrophobic Forces.
  4. Do proteins fold into a conformation of lower or highest energy?

    What determines the particular three-dimensional structure of proteins?

    The final folded structure, or _______ adopted by any polypeptide chain is determined by energetic considerations: a protein generally folds into the shape in which its fee energy (G) is _________.

    How is the folding process energetically favorable?

    The sequence of amino acids in its polypeptide chain.

    Conformation, minimized.

    It releases heat and increases the disorder of the universe.
  5. A protein can be unfolded, or _________, by treatment with solvents that do what?

    What does this treatment convert the protein into?

    When the solvent is removed, Protein often refolds spontaneously into its original conformation--a process called ___________.

    In regards to the renaturation, what does it mean for information necessary to specify the three-dimensional shape?
    Disrupt the non covalent interactions holding the folded chain together.

    A flexible polypeptide that lost its neutral shape.

    The instructions are housed in the sequence of amino acids.
  6. Can a protein chain fold into its correct conformation without outside help?

    Protein folding in a living cell is generally assisted by specialized proteins called _________.

    What do the chaperones usually bind to and how do they help them (hint: kinetics)?

    Chaperones merely do what (2 things)? What is their input of energy source?

    How do they cause folding (2 ways)?

    Chaperone proteins.

    Partly folded chains and help them to fold along the most energetically favorable pathway.

    Make protein folding more efficient and reliable. Hydrolysis

    Associating directly to the protein or serving as a barrel with a cap.
  7. ________ was found in the protein alpha-keratin.

    What is alpha-keratin found in?

    A second folded structure, called a ________, was found in the protein _________, the major constituent of silk.

    What causes the two folding patterns between what two groups in the polypeptide backbone?
    • alpha helix.
    • Skin, hair, nails, and horns.
    • beta sheet, fibroin
    • Hydrogen bonding between carbonyl and amino groups in the polypeptide backbone.
Card Set
Protein shape part one
part one of protein structure and function
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