Lecture 1 Flashcards

1
Q

Give examples of macromolecules

A

lipids, carbohydrates, nucleic acids and proteins

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2
Q

What are structural proteins

A

-they provided mechanical support to cells and tissues e.g. collagen and elastin form tendons and ligaments

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3
Q

What are motor proteins

A

-they generate movement in cells and tissues eg. myosin in skeletal muscle cells provide the motive force for humans to move

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4
Q

What are signal proteins

A

-they carry extracellular signals from cell to cell
e.g. many of the hormone and growth factors that coordinate physiological functions in animals are protein e.g. insulin

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5
Q

What are transport proteins

A

-they carry small molecules or ions
e.g. in the bloodstream serum albumin carries iron
-many proteins embedded in cell membranes transport ions or small molecules across the membrane

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6
Q

What are gene regulatory proteins

A

-they bind to DNA to switch genes on or off
-the lactose repressor in bacteria silences the genes for enzymes that degrade the sugar lactose

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7
Q

What are receptor proteins

A

-they detect signals and transmit them to the cells response machinery
e.g. rhodopsin in the retina detects light: the acetylcholine receptor in the membrane of a muscle cell is activated by acetylcholine released from a nerve ending

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8
Q

What are special purpose proteins

A

-they are highly variable
e.g. organisms make many proteins with highly specialised properties
-these molecules illustrate the amazing range of functions that proteins can perform

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9
Q

What are proteins made out of?

A

-amino acids

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10
Q

Describe the structure of an amino acid?

A

-amino acids are linked end to end by covalent bonds in linear chains

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11
Q

What is a polypeptide?

A

-an amino acid chain

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12
Q

What is the structure of a polypeptide?

A

-polypeptides are folded into specific 3D shapes

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13
Q

What is formed when one more more polypeptides fold together?

A

-a protein is formed

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14
Q

What can a primary structure be described as?

A

a linear amino acid sequence

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15
Q

What can a secondary structure be described as?

A

-a polypeptide folds into regular shapes, different secondary structures can pack together to form domains

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16
Q

What can a tertiary structure be described as?

A

-the arrangement of one / multiple domains
-this results in a 3D structure

17
Q

What can a quaternary structure be described as?

A

-the arrangement of multiple polypeptides
-this results in a protein complex with multiple subunits

18
Q

What complexes are in an amino acid?

A

-the amino group (NH2)
-the alpha carbon
-the carboxyl group
-the side chain(R)

19
Q

What is a zwitterion?

A

-an amino acid is a Zwitterion at pH7
-it has both positive and negative charges

20
Q

Are amino acids chiral or achiral?

A

-amino acids are chiral, thus their image cannot be superimposed
(except glycine - as the sidechain of glycine is H)

21
Q

Where are L amino acids found?

A

-L amino acids are found in proteins, in nature

22
Q

What are examples of small and simple amino acids

A

-Glycine (Gly, G) and Alanine (Ala, A)

23
Q

What are examples of amino acids with bulky, hydrophobic side chain?

A

-Valine (Val, V), Leucine (Leu, L), Isoleucine (Ile, I) and Methionine (Met, M)
-as these amino acids are hydrophobic they tend to be buried ‘inside’ the protein

24
Q

Describe the amino acid Cysteine

A

-(Cys, C)
-contains a thiol (-SH) group which allows it to form a disulphide bond

25
Q

Give examples of amino acids with aromatic (ring) side chain?

A

Phenylalanine (Phe, F), Tyrosine (Try, T) and Tryptophan (Trp, W)

26
Q

Give examples of amino acids with polar side chain(s)

A

(amino acids with polar side chains contain a hydroxyl (OH) group)
e.g. Serine (Ser, S) and Threonine (Thr, T)

27
Q
A