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amino acids
| Question | Answer |
|---|---|
| amino acids monomers are used by which type of bonds | peptide |
| Name the 4 types of atoms in a peptide bond. | carbon, hydrogen, oxygen and nitrogen |
| Name the 4 types of amino acids | acidic, basic, polar and non polar amino acids |
| State the 4 groups around the central carbon in an amino acid | hydrogen, acidic COOH, basic NH2 and an R group |
| Which group varies between the 20 different amino acids | R group |
| Name 3 differences between R group | size, shape, charge, hydrogen bonding capacity & chemical reactivity |
| Which type of amino acids are found on the surface of the membrane | hydrophilic amino acids |
| Which type of amino acids are found in the centre of the membrane with the phospholipid tails | hydrophobic amino acids |
| The primary level of protein structure is the | sequence of amino acid |
| The secondary level of protein structure is | hydrogen bonding along the BACKBONE |
| Name 2 types of secondary structure | alpha helix, beta pleated sheets & turns |
| Describe the tertiary level of protein structure | Different types of interactions between amino acid R groups causing further folding into 3D shape |
| State 3 types of tertiary R group interactions | disulfide bridge, ionic bonds, hydrogen bonding, hydrophobic interactions and london dispersion forces |
| Describe the difference in hydrogen bonding between secondary and tertiary levels. | secondary = along backbone (COOH & NH2) of amino acids tertiary = R groups of amino acids |
| What is meant by a disulfide bridge | covalent bond between two sulfur atoms |
| Define the quaternary structure of a protein | Spatial arrangement of two or more connected polypeptides |
| What is meant by a prosthetic group. | non protein part required for its function. |
| Describe the quaternary structure of haemoglobin and its prosthetic group | haemoglobin = 4 subunits with Iron prosthetic group to make haem for oyxgen binding/release. |
| State two factors that can affect R group interactions at the tertiary level. | 1. pH 2. temperature |
| Which type of R group interactions are affected when proteins are denatured by temperature. | Any of the interactions. disulfide bridge, ionic bonds, hydrogen bonding, hydrophobic interactions and london dispersion forces |
| Which type of R group interactions are affected when proteins are denatured by pH | Ionic interactions. Reversible denaturing if pH altered as bonds form again. |
| Which type of proteins are on the surface of the membrane | peripheral |
| Which type of proteins are inserted into the membrane | integral |
| Which type of protein has mainly hydrophilic amino acids in the protein | peripheral |
| Describe the location of amino acids in an integral protein | surface = hydrophilic middle = hydrophobic |
| Which type of interactions do hydrophilic amino acids in peripheral proteins make | ionic or hydrogen bonds |
| Which type of interactions do non polar amino acids in the middle of membranes make | hydrophobic interactions |
| interactions between spatially distinct sites in multi subunit are termed | allosteric protein |
| Define co operativity in allosteric proteins. | whereby changes in binding at one subunit alters the affinity of the remaining subunits. |
| Name two factors that affect affinity of haemoglobin for oxygen. | 1. pH 2.temperature |
| State whether high or low pH/temperature causes oxygen to be released to the tissues | high temperature & low pH |
| State what is meant by a ligand | A molecule that can bind to complementary R groups on proteins. |
| When R groups on proteins bind to ligands they do so as they are complementary in terms of | shape OR chemistry |
| When ligands bind to R groups on proteins this causes a | conformational change in protein structure affecting its function. |
| In haemoglobin disocciation curve graphs a left shift is caused by | increased pH and lower temperature |
| The further to the right the _________ the affinity the haemoglobin has for oxygen. | lower |
| State the term for the site of modulators away from the active site | allosteric site |
| when a molecule binds away from the active but increases the binding of the substrate for the active site the molecule is called | a positive modulator |
| Name one type of post translational modification at the golgi apparatus apart from addition of carbohydrate | phosphorylation of proteins |
| The transfer of a phosphate group to R groups on proteins is catalysed by which enzyme | kinase |
| Which reaction is catalysed by phosphatase | dephosphorylation |
| State the impact of phosphorylating/dephosphorylating a protein | conformational change in protein shape activating or deactivating protein |
| Is phosphorylation an irreversible process | no reversible with a phosphatase |
| Adding a phosphate increases a) positive b) negative charge | negative charge |
| Which type of R group interactions are affected by adding or removing negatively charged phosphate | ionic interactions |
| State a type of protein activated or deactivated by phosphorylation or dephosphorylation | enzymes OR receptors OR Rb (deactivated cell cycle) |
Created by:
brightminds