Unit 3 Science Investigation Skills

Slides:



Advertisements
Similar presentations
Proteins Review. Learning outcomes (e) Describe the structure of an amino acid and the formation and breakage of a peptide bond. (f) Explain the meaning.
Advertisements

Pp 50 – 51 & Pp 15 & Proteins Proteins are polymers of amino acids Each has a unique 3D shape Amino acid sequences vary Proteins are.
Proteins. What are Proteins? The most complex biological molecules Contain C, H, O and N Sometimes contain S May form complexes with other molecules containing.
Proteins are all made from chains of amino acids.
Protein Structure & Function
1. Primary Structure: Polypeptide chain Polypeptide chain Amino acid monomers Peptide linkages Figure 3.6 The Four Levels of Protein Structure.
Homework for next week Green q 1,2,3 p29 Do evaluation points from Biuret Practical Revise test on all work next week Bring evidence you have revised please.
Proteins – p. 25
Lesson 5.  Explain the term secondary structure  Explain the term tertiary structure.
Biomolecules: Nucleic Acids and Proteins
Proteins R R O O H H N C C N C C H H OH H H OH
7.5: PROTEINS Proteins Function Structure. Function 7.5.4: State four functions of proteins, giving a named example of each. [Obj. 1] Proteins are the.
Topic 7.5 Proteins (AHL).
PROTEINS. Learning Outcomes: B4 - describe the chemical structure of proteins List functions of proteins Draw and describe the structure of an amino acid.
General Info about Proteins Most diverse and most important macromolecules. Our entire DNA codes for proteins only, and nothing else. Therefore they are.
Primary structure. Proteins Proteins contain Carbon (C), Hydrogen (H), Oxygen, Nitrogen (N) and sometimes Sulphur (S) The monomer units of proteins are.
The Structure of Proteins. Functions of Proteins Fibrous proteins – structural, e.g. collagen. Globular proteins – metabolic functions, e.g. haemoglobin.
Proteins Biochemistry Unit 1. What You Need to Know! How to recognize protein by its structural formula The cellular function of proteins The four structural.
Protein Recap. Protein Syllabus Draw the general amino acid structure.
PROTEINS Have a wide range of functions; haemoglobin, antibodies & enzymes Amino acids are the monomers Twenty naturally occurring amino acids The order.
Biological Molecules: Proteins  Links to GCSE  Bonding  Balanced diet & food tests  Hormones & immunity  Haemoglobin.
Amino Acids. Starter Name the functions of proteins in the human body.
Denaturation of proteins Some of the interactions responsible for holding a protein in its 3D tertiary structure are weak –Eg hydrogen bonds They are easily.
This diagram shows the primary structure of PIG INSULIN, a protein hormone as discovered by Frederick Sanger. He was given a Nobel prize in The primary.
Haemoglobin: Structure and Formation of Proteins 1.1.2, a, b,c.
Lesson 6.  Textbooks  Repro  Page 8-9 of ppq  Comparison sheet.
Proteins Proteins are the building materials for the body.
19.5 Protein Structure: Tertiary and Quaternary Levels
Biology Induction.
St Philip Howard Catholic High School AS Biology bridging work 2016
Functional Variety of Proteins
The BIG FOUR!.
Protein Proteins are found throughout living organisms.
Proteins What do we need proteins for?
Each amino acid shares a common structure, with an amine group (NH2),
Proteins have a very wide range of functions in living organisms.
Proteins and Nucleic Acids
(4) Genes and proteins in health and disease
Living By Chemistry SECOND EDITION
Proteins: Secondary and Tertiary Structure
Protein Structure Amino Acids Polypeptide Levels of Structure
Proteins.
Amino Acids and Proteins
Primary, secondary, tertiary and quaternary structures.
Chapter 2.4: Proteins.
Proteins Topic 7.5.
Proteins Basic structure of an amino acid
PROTEINS AHL Topic 7.5 IB Biology Miss Werba.
Proteins.
Proteins Topic 7.5.
The Chemistry of Life Proteins
Chapter 19: Proteins.
Protein Structure Chapter 14.
What is they, what makes them etc
Proteins Describe what a protein is and give examples of what they are used for. Describe the structure and shape of the different types of proteins. Explain,
Proteins Ms Glasgow.
SPH Sixth Form AS Biology Bridging Work
Protein Shape & Function
Proteins.
PROTEINS Unlike Carbohydrates and Fats, which are primarily used as an energy source; Proteins are primarily used to structurally build and repair the.
Draw the structure of an amino acid
AMIDES.
Presentation transcript:

Unit 3 Science Investigation Skills Topic D: Enzymes in action Lesson 1

Learning objectives To become familiar with assessment command words To gain awareness of the method of assessment for Unit 3 To describe peptide linkage of amino acids To research the different levels of protein structure and the types of bonds involved To relate protein structure to function

Command words There are many command words that are used to tell you what you need to do in the assessment tasks. You need to have a firm understanding of the specific meanings of the command words used in assessments. The command words required are defined in the specification and you should make sure you know what they are asking you to do.

Example command word: ‘compare’ The definition of ‘compare’ in the specification is as follows: You need to look for the similarities and differences of two (or more) things. The answer must include at least one similarity and one difference. This should not require the drawing of a conclusion. The answer must relate to both (or all) things mentioned in the question. Practice task: Compare sheep and rabbits, following the above definition. You could ask a friend to check you have included all the requirements for a good comparison, and have left out points not required.

How will you be assessed on this unit? Unit 3 is an externally assessed unit. The assessment consists of two parts: Part A: You will carry out an investigation following a task brief provided by Pearson. You will have two weeks to do this. You will need to plan, carry out and record a scientific investigation to create primary data (results/observations) for use in Part B. You will not be assessed on practical competence. Part B: This takes place in May or June, two weeks after beginning part A. Part B is a written task worth 60 marks. You will have 1½ hours to complete a task booklet in which you will process, analyse and evaluate your primary data and secondary data. Sample assessment materials will be available for you to practise your skills.

What are the functions of these substances in the body? keratin enzymes haemoglobin hormones collagen antibodies

What do all of these substances have in common? They all consist of protein. keratin enzymes haemoglobin (some) hormones collagen antibodies

Proteins consist of long chains of amino acids (polypeptides). Figure 5.21 p. 78 Biology 3rd Edition Campbell Benjamin/Cummings ISBN 0-8053-1880-1

Structure of an amino acid The central carbon atom of an amino acid is bonded to a hydrogen atom and three other groups. Figure after © 2010 PJ Russell, iGenetics 3rd ed.; all text material © 2011 by Steven M. Carr

Build a model of an amino acid using a hydrogen atom for the R group as an example. Figure after © 2010 PJ Russell, iGenetics 3rd ed.; all text material © 2011 by Steven M. Carr

Amino acids are joined together by peptide bonds which form between the carboxyl group of one amino acid and the amino group of another. A molecule of water is lost, so this is a condensation reaction. Image taken from : © 2010 PJ Russell, iGenetics 3rd ed.; all text material © 2011 by Steven M. Carr

How long a polypeptide chain can your class make? The amino acid glycine has an R group consisting of a hydrogen atom. Add this to your model to form a glycine molecule. Working with a partner, link two glycines together by removing H2O and form a peptide bond between them. Image taken from : © 2010 PJ Russell, iGenetics 3rd ed.; all text material © 2011 by Steven M. Carr How long a polypeptide chain can your class make?

Different R groups assign different properties to the amino acids Different R groups assign different properties to the amino acids. There are four main types of amino acids with properties determined by their R groups: Polar/hydrophilic Non-polar/hydrophobic Acidic/negatively charged R groups Basic/positively charged R groups

Polar R groups are hydrophilic and non-polar R groups are hydrophobic. Test your understanding In a soluble blood protein, which type of amino acid would you expect to find on the external surface of the protein molecule (exposed to the water-containing plasma)? Which type of amino acid would you expect to find embedded within the internal part of the molecule?

Some R groups have a negative charge (acidic, eg Some R groups have a negative charge (acidic, eg. COO-) and some have a positive charge (basic, e.g. NH3+). From the five amino acids shown below, can you choose two that might be attracted to each other and pulled together in a protein structure?

Different types of bond form between different types of amino acid R groups within a protein.

Research activity Protein structure is described at three levels: primary, secondary and tertiary. Use books and Internet sources to find out about these levels of structure and identify: the structural features involved at each level the types of R groups, attractions and bonds involved in holding these structural features together. Extension questions Some proteins have a further level of structure. What is this called and what does it involve? Can you identify any examples of proteins with this level of structure?

The different amino acid R groups: cause a chain of amino acids (polypeptide chain) to fold into a particular shape assign properties that enable the protein to carry out its function in a living organism. Protein shapes come in two main forms: fibrous and globular. Fibrous Globular

Fibrous proteins are insoluble in water and have strong, elongated structures. Globular proteins are soluble in water and have more rounded structures. Can you sort these proteins into the two groups? elastin fibrous globular