2.9 Proteins Flashcards
2.9 i) Know the basic structure of an amino acid. ii) Understand the formation of polypeptides and proteins. iii) Understand the significance of a protein’s primary structure in determining its three-dimensional structure and properties. iv) Know the molecular structure of a globular protein and a fibrous protein and understand how their structures relate to their functions (including haemoglobin and collagen). (22 cards)
What are proteins?
polymers made of amino acids (the amino acids are monomers)
Proteins examples:
- enzymes
- hormones
- antibodies
What is a dipeptide?
formed when two amino acids join together
What is a polypeptide?
formed when more than two amino acids join together
What is the basic structure of an amino acid?
H
|
.. NH2 - C - COOH
|
R
(ignore the dots - only for formatting)
Identify the chemical groups in an amino acid:
NH2 - amine
R - carbon-containing variable side group (different for each amino acid)
COOH - carboxyl group
How many amino acids are there?
20
What do you call the amino acids that animals have to obtain through their diet?
essential amino acids
How are polypeptide chains formed?
- amino acids are joined by condensation reactions
- the OH on the COOH and the H on the NH2 are lost to form water
- the bond forms between C and N
What are the bonds between amino acids called?
peptide bonds
What is the primary structure of a protein?
the sequence of amino acids in the polypeptide chain
What is the secondary structure of a protein? How does it form?
- hydrogen bonds form between amino acids in the polypeptide chain
- this causes the polypeptide chain to either
- coil into an alpha helix (like an extended spring)
- or fold into a beta pleated sheet
What is the tertiary structure of a protein?
- the polypeptide chain further bends and folds into a precise 3D structure
- this is due to the bonds that form between amino acids in the polypeptide chain
- the further bending and folding also depends on the polarity of the R groups: polar R groups face inwards (away from water) and non-polar R groups face outwards (towards water)
- the bonds that form include:
ionic bonds
chemical bonds e.g. disulfide bonds
more hydrogen bonds - for proteins made from a single polypeptide chain, their tertiary structure forms their final 3D structure
Describe the ionic and disulfide bonds that form at the tertiary structure of a protein:
- ionic bonds: the electrostatic attraction between oppositely charged ions (some R groups ionise, and so ionic bonds can form)
- disulfide bonds: covalent bonds that form between a sulfur atom on one cysteine (amino acid) and a sulfur atom on another cysteine
What is the quaternary structure of a protein?
- some proteins are made of several different polypeptide chains held together by bonds
- the quaternary structure forms when different polypeptide chains assemble together
- e.g. haemoglobin, insulin, collagen
What are conjugated proteins?
proteins containing another chemical group called a prosthetic group (a group that is not part of an amino acid)
e.g. iron group in haemoglobin
State the bonds that form at the different structural levels of proteins:
- primary structure: peptide bonds
- secondary structure: hydrogen bonds
- tertiary structure:
ionic bonds
disulfide bonds (and other chemical bonds)
hydrophobic and hydrophilic interactions
hydrogen bonds - quaternary structure: all of the above
What is the significance of a protein’s primary structure in determining its three-dimensional structure and properties?
- the primary structure of a protein is the amino acid sequence in a polypeptide chain
- this sequence determines what types of bonds will form
- e.g. disulfide bonds will form if cysteines are present in the amino acid sequence
- the types of bonds and where these bonds form will determine how the polypeptide chain folds
- and so will determine its 3D structure/shape
- the 3D structure of the protein then determines its properties and its function in the body
What are globular proteins? What are their properties?
- spherical, compact proteins made up of multiple polypeptide chains
- they are soluble and so can be easily transported in fluids: this is because the hydrophilic parts of the chains face outwards and the hydrophobic parts of the chain face inwards
- their 3D structures are crucial for binding to other substances
What are examples of globular proteins? Explain how their 3D structures are important:
- e.g. haemoglobin: a globular protein made of 4 polypeptide chains. its solubility means it can be easily transported in the blood. this is important because it is responsible for transporting oxygen. the iron-containing haem groups present bind to oxygen
- e.g. enzymes: their 3D structures are crucial for catalysing reactions
What are fibrous proteins? What are their properties?
- proteins made of long, insoluble polypeptide chains that coil tightly to each other to form a rope like shape
- the chains are held together by lots of bonds (e.g. disulfide and hydrogen bonds) - this makes them strong
- cross links between chains add additional strength
- often found in supportive tissue due to their strength
What are examples of fibrous proteins? Explain how their 3D structures are important:
- e.g. collagen: a strong, fibrous protein that forms connective tissue in animals. its 3D structure is important as it provides strength
- e.g. keratin: found in hair, nails, and skin