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Doc
Brown's Chemistry Clinic
My unofficial
support for Salters
A2
Advanced Chemistry
Salters A2 Chemistry - EP
"Engineering Proteins"
Unit map and learning objectives list
- part of module 2849
* My
revision index * EP exam bashing thought
* extra DP backup help *
My Salters AS homepage *
My Salters A2 homepage *
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PLEASE REMEMBER, THESE ARE NOT 'STAND ALONE' NOTES, and were designed for my
classes for use alongside the Salters resources - Chemical Ideas, Chemical
Storylines, Practical Activities-Investigations and the AS-A2 Revision guides
all published by Heinemann Secondary Series, to reduce the reading workload and
offer a study strategy. From your
teacher (not me!), its handy to have the answers to the Chemical Ideas,
Storylines Assignments and Activities Questions side by side with the texts and
these strategy pages. You haven't time to redo the Q's but a quick read of the
Q's and connecting with the official answers is valuable revision. |
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EP2.1 Investigating amines and amino acids
EP2.2 What's in aspartame?
EP2.3 Using NMR spectroscopy for structure
determination
EP2.4 The shapes of alpha-amino acids
EP2.5 A testing smell
EP2.6 Taking note of proteins
EP2.7 Modelling DNA
EP2.8 Life reveals its twisted secret |
EP2 Protein Building |
13.3 Carboxylic acids and their
derivatives (revision)
13.4 The -OH group in alcohols, phenols
and acids (revision)
13.8 Amines and amides (revision)
13.9 Amino acids
6.6 Nuclear magnetic resonance
spectroscopy (NMR)
3.3 Shapes of molecules (revision)
3.5 Geometric isomerism (revision)
3.6 Optical Isomerism |
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EP6.1 Testing for glucose
EP6.2 S Succinate dehydrogenase
EP6.3 The effect of enzyme and substrate
concentration on the rate of reaction
EP6.4 Using the iodine clock method to
find the order of a reaction
EP6.5 Enzyme kinetics |
EP6 Enzymes |
10.2 The effect of temperature on rate
(revision)
10.5 How do catalysts work? (revision)
10.3 The effect of concentration on rate |
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Unit
EP Learning Outcomes
KEY: CS = Chemical
storylines, CI = Chemical Ideas, Act = Activity: be
able to
- O recall that
proteins are condensation polymers formed from amino acid
monomers; [CS EP2; CI 13.9]
- O recognise and describe the generalised
structure of amino acids (compare with amines, and note two functional
groups in molecule); [CS EP2 Ass 1/2; Act EP2.1/2.4; CI 13.3/13.4/13.8/13.9]
Please remember you asked about ANY organic functional group previously
encountered - all so far on homologous
series/functional Group page and WM
quiz helps
- O describe the
acid-base properties of amino acids (via
the two functional groups -NH2 and -COOH) and the formation of zwitterions; ; [Act EP2.1; CI 13.3/13.4/13.8/13.9]
- O describe the
structure, formation and hydrolysis*
of the peptide link between amino acid residues in
proteins
(*H2O, reflux HCl or NaOH catalyst, equations)
and know the terms dipeptide (be
aware of two isomers depending on order) and polypeptide; [CS EP2 Ass 2; Act EP2.2; CI 13.9]
* and this may be the 1st stage in (i) analysing a polypeptide via
paper chromatography, (ii) the isolation and purifying by crystallisation
of acids (x-ref nylon hydrolysis), involves the techniques of reflux, reduced
pressure filteration, recrystallisation and melting point determination as a
simple purity test or 'superficial' identification.
- O explain the
importance of amino acid sequence in determining the structure and properties of proteins, and account for the diversity of proteins in living things; ; [CS EP1/2]
- O recognise
stereoisomers: both cis-trans geometrical isomerism and optical isomers (enantiomers);
structural isomers and analyse for all bond angles; [Act EP2.4/2.5; CI 3.3/3.5/3.6]
- O explain and use the term ‘chiral’ as applied to a molecule;
[CS EP2; Act EP 2.4/2.5; CI 3.3/3.6]
- O build models and draw and interpret
diagrams to represent optical isomers of simple molecules; [Act EP 2.4/2.5; CI 3.3/3.6]
- O describe how
nuclear magnetic resonance spectroscopy* (n.m.r. or NMR) can be used for the elucidation of molecular structure; [Act EP 2.3; CI 6.6]
* interpretation of chemical shift peaks (wrt TMS standard)
in terms of (i) different 'proton environments' and (ii) their ratio
related to the numbers of protons in a particular bonding situation
- O interpret nuclear magnetic resonance spectra for simple compounds given relevant information (reference to splitting of the resonances is not required);[Act EP 2.3; CI 6.6]
- O write an
expression for the equilibrium constant, Kc, for a given
homogeneous reaction and quote the appropriate units; [CS EP5 Ass 8; CI 7.1/7.2]
- O describe the way in which changes of
temperature and pressure affect the position of an equilibrium and the
magnitude of the equilibrium constant; [CI 7.1/7.2]
- O use values of
Kc, together with given data on equilibrium concentrations, to
calculate the composition/concentrations of equilibrium mixtures or
given [concentration] data calculate Kc (and units) [CI 7.1/7.2]
- O distinguish between the
primary (amino acid residue sequence), secondary
(helix or sheet), tertiary structure
(folded into final 3D shape) and quaternary
(multiple combinations of tertiary) of proteins; [CS EP2/4]
- O explain the role of
hydrogen bonds and other intermolecular forces
(permanent dipole - permanent dipole, instantaneous dipole - induced dipole)
in determining the structure and properties of
proteins; [CS EP2/4; CI 5.3/5.4] covalent and
ionic bonding can also be involved in 'holding' separate strands or
sections a polypeptide together
- O describe the
double helix structure of DNA in terms of a sugar-phosphate backbone and attached bases,
see LO 17 (recall of detailed structure is not required); [CS EP2/3 Ass 3; Act EP 2.7/2.8(history)]
- O explain the significance of
hydrogen bonding in the pairing of bases in DNA, and relate to the replication of genetic information; [CS EP2 Ass 4/5/6; Act EP 2.7/2.8(history); CI 5.4]
- O explain
how DNA encodes for the amino acid sequence in a protein [CS EP2; Act EP
2.7/2.8 (history)]
- O use empirical
rate equations of the form: rate = k[A]m [B]n where m and n are integers (0, 1 or 2); [Act EP 6.4; CI 10.3]
- O explain and use the
terms: rate of reaction, rate constant, order of reaction (both overall and with respect to a given
reagent eg a reactant or a catalyst) [Act EP 6.4/6.5; CI 10.3]
- O describe
some experimental
methods* for measuring the rate of
reactions [Act EP 6.3/6.4/6.5; CI 10.3] * eg
sketch/describe apparatus to collect and measure the volume of oxygen from the
catalase catalytic decomposition of hydrogen peroxide.
- O use experimental data* to find the order of a reaction (zero, first or second
order) [Act EP 6.5/6.5; CI 10.3] * eg from (i)
graphs of gas volume versus time for different concentrations and measure
initial rate (ii) gas volume versus time and measuring 'half-life
volumes' and if constant proves 1st order kinetics and (iii) change in
solution concentration e.g. 'decay' curve of reactant or 'formation' curve of
product.
- O use given data to
calculate half-lives* for a reaction; [CI 10.3]
* if constant shows 1st order kinetics, and know how
such data can be used to predict the 'residue' after a certain time interval
- O show awareness of the
industrial importance of enzymes; ; [CS EP 6]
- O describe and explain* the characteristics of enzyme catalysis, including: (i)
specificity, (ii) temperature, (ii)
pH sensitivity, (iii) inhibition and (iv) concentration
factors (usually 1st order wrt substrate and enzyme,
but can be zero for substrate at high concentrations when rate becomes
diffusion dependant) [CS EP6; Act EP
6.1/6.2/6.3/6.4/6.5; CI 10.2/10.5] * eg via applying
rates factors or the molecular structural features of the enzyme (key and lock
mechanism)
- O account for the
specificity of enzymes in terms of a simple ‘lock and key’ model of enzyme action; [CS EP 6; Act EP 6.2; CI 10.5]
- O explain in outline the technique of ‘genetic engineering’; [CS EP 3/5 Ass 7]
eg modifying DNA of an organism so it produces a specific enzyme to
'transform' a specific molecule to a desired product
- O discuss
applications of genetic engineering techniques and be able to
quote advantages and disadvantages of GM [CS EP1/3/4/5]
GENERAL
REVISION
NOTES
* Salters
Advanced Level Chemistry * Salters Advanced Level Chemistry * Salters
Advanced Level Chemistry * Salters Advanced Level Chemistry * Salters
Advanced Level Chemistry *
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