MGD S1 - Cell structure, Amino acids and Proteins Flashcards Preview

Semester 1 > MGD S1 - Cell structure, Amino acids and Proteins > Flashcards

Flashcards in MGD S1 - Cell structure, Amino acids and Proteins Deck (35):
1

Ribosome function?

Ribosomes interpret cellular information from the nucleus and synthesise proteins. There are different types of ribosomes (80s eukaryotic, 70s prokaryotic)

2

Microfilament function?

- Made up of actin

- In non-muscle cells the actin makes up a web-like layer, the cell cortex, located immediately below the cell's plasma membrane

- The structure helps define the shape of the cell

- They also facilitate the movement of certain particles and structures i.e macrophages, fibroblasts and nerve growth cones

3

Microtubules function?

- Made ups of α-tubulin and β-tubulin dimers

- dynamic structure

- The main 'building blocks' forming the cytoskeleton

- The cells framework within which all components of the cell are held in position or allowed restricted movement

- Movement of materials and structures within cells Eg help form the mitotic spindle during prophase

4

Intermediate filament function?

- Important for maintaining the mechanical structure of cells

- There are different types occurring in different cells and therefore provide structural support in slightly different ways

5

Centrosome function?

Contain the centrioles, which are involved in the process of mitosis

6

Nucleus function?

- Control centre of the cell

- Contains cell's DNA in the form of genes

- Sequestration of DNA and replication of DNA

- Transcription and modification of RNA

7

Rough endoplasmic reticulum function?

- Consists of many interconnected membranous sacs called cisternae, onto which ribosomes are attached In the lumen of the cisternae.

Produce proteins that are either:

1) Retained within vesicles

2) Secreted from the cell

8

Smooth endoplasmic reticulum function?

- Many enzymes attached to the surface of the the cisternae or located within Chemical reactions within the SER vary with the type and location of cells

- Helps with protein folding

- Glycosylation - involves the addition of oligosaccharides

- Disulphide bond formation and rearrangement - to stabilise the tertiary and quaternary structure of many proteins

- Modification of some drugs EG by the cytochrome P450 enzyme in liver cells

9

Lysosome function?

1) Autophagy - Digestion of materials within the cells

2) Heterophagy - Digestion of materials originating from outside the cell

3) Biosynthesis - recycling unwanted products of chemical reactions to process materials received from outside the cell Lysosomes also destroy the cell - usually after it has dies

10

Peroxisome function?

Similar to lysosome but also include:

- β-oxidation of fatty acids

- Breakdown excess purines to urea

- Breakdown of toxic compounds Eg in the cells of the liver and kidney

- Plays a role in the biosynthesis of cholesterol and bile acids derived from cholesterol

11

Vesicle function?

Transport and deliver contents (hormones and neurotransmitters etc) either into or out of the cell, via the cell membrane

12

What are the 4 types of non-covalent interactions that help bring molecules in a cell together?

1) Electrostatic interaction - attractive forces between oppositely charged atoms

2) Hydrogen bonds - special form of polar interaction where an electropositive hydrogen atom is partially shared by two electronegative atoms. It hydrogen can be seen as a proton that has partially disassociated from a donor atom, allowing it to be shared by a second acceptor atom

3) van der Waals attractions - Spontaneous polar interactions

4) Hydrophobic interaction - caused by pushing of non-polar surfaces out of the hydrogen-bonded water network, where they would interfere with the highly favourable interactions between water molecules

13

How many amino acids are there?

20

14

How are amino acids linked?

Covalent peptide bonds

15

Define aliphatic

Hydrocarbons arranged in a linear chain

16

Define aromatic

Closed hydrocarbon chain

17

What is an amphipathic molecule?

Molecule containing both hydrophilic and hydrophobic regions

18

Define pH

Concentration of H+ ions in solution pH= -log(H+)

19

What is the purpose of a buffer?

Solution made of weak acid and its conjugate base that resists changes in pH upon the addition of small amounts of acid or alkali

20

What is the isoelectric point of a protein?

pH at which the protein has no net charge Acidic proteins have a low Pi and basic protein have a high Pi

21

Describe the structure of an amino acid

- Central alpha carbon atom

- Amino group

- Carboxyl group

- R group

22

What happens to an amino acid with a Pi lower than the pH of solution?

Amino acid is deprotonated

23

How are amino acids classified?

Polar, non-polar, aliphatic, aromatic, charged, uncharged

24

Name two non-polar amino acids?

Phenylalanine and Tryptophan

25

Name two negatively charged amino acids

Glutamate and aspartate

26

Name two positively charged amino acids

Lysine and arginine

27

What is a peptide bond? List the features of a peptide bond

- Covalent linking of two amino acids between the carboxyl group of one and the amino group of the other with the subsequent removal of a water molecule

- Peptide bonds are planar, in trans arrangement and have double bond properties due to delocalisation of electrons

28

What is the consequence of a change in the primary structure of a protein?

Altering the sequence of amino acids can impact the secondary and tertiary structure leading to a non-functional polypeptide

29

List the key features of an alpha helix

1) Right handed

2) R groups on the outside of the helix

3) 3.6 amino acids per turn

4) 0.54 nm pitch

5) Stabilised by hydrogen bonds

30

List the key features of a beta pleated sheet

1) Extended conformation

2) Parallel or antiparallel

3) Interconnecting hydrogen bonds between each

4) R groups alternate between opposite sides of the chain

5) 0.35nm pitch

31

Name two helix forming amino acids

Alanine and leucine - small hydrophobic residues

32

Name two helix breaking amino acids

Glycine - Small R groups support other conformation

Proline - non-rotation around C-N bond

33

List the essential amino acids

If Learnt, This Huge List May Prove Truly Valuable

Isoleucine Leucine Tryptophan Histidine Lysine Methionine Phenylalanine Threonine Valine

34

Describe the differences between globular and fibrous proteins and give examples of each

Globular - different secondary structures, compact, for catalysis and regulation Eg enzymes

Fibrous - One type of secondary structure, long strands or sheets, for shape and support Eg collagen

35

What are amyloidosis?

Accumulation of mis-folded or altered dysfunctional proteins which cause disease