Brainscape's Knowledge GenomeTM

Browse over 1 million classes created by top students, professors, publishers, and experts.


See full index

Chemistry > Biochemistry > Flashcards

Biochemistry Flashcards

You may prefer our related Brainscape-certified flashcards:
Chemistry 101 flashcards Periodic Table flashcards AP® Chemistry flashcards Organic Chemistry 101 flashcards
1
Q

Structure of an amino acid

A

Amino group (NH2), alpha carbon, hydrogen, carboxylic acid group (COOH), variable side chain (R)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

Functional groups of an amino acid

A

An amine group (-NH2) and a carboxylic acid acid (COOH)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

How do naturally occurring amino acids differ

A

The R group

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

Which amino acid isn’t optically active

A

Glycine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

Why are amino acids optically active

A

They have a chiral carbon

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

Which which optical isomer naturally occurs and what is the effect on plane polarised light

A

L-isomer rotates plane polarised light anti-clockwise (the left)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

Can amino acid acids act as a base or an acid

A

Both an acid and a base

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

Does an amino acid act as an acid or a base in a solution of acid

A

Base

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

Does an amino acid act as an acid or a base in a solution of base

A

Acid

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

Does an amino acid act as an acid or a base in a solution of isoelectric pH

A

Zwitterion so both

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

Which part of an amino acid accepts a proton

A

The lone pair on the NH2

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

Which part of the amino acid donates a proton

A

Carboxylic acid

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

What is the isoelectric point

A

pH at which is has no net charge. Midway between two pKa of its two functional groups

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

Which amino acid has the variable group H

A

Glycine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

Charge on an amino acid in a acidic solution

A

Positive

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

Are cations positive or negative

A

Positive

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

What binds join amino acids in a protein

A

Peptide

18
Q

What sort of polymers are proteins

A

Condensation polymers

19
Q

Define fibrous proteins

A

Long chains of polypeptides found in bundles and insoluble in water

20
Q

Define globular proteins

A

Polypeptide chains folded into roughly spherical shapes that are soluble in water

21
Q

Example of globular protein

A

Haemoglobin

22
Q

Example of fibrous protein

A

Keratin

23
Q

Define primary structure

A

The order of alpha-amino acids in a protein

24
Q

How do you determine the order of amino acids in a protein

A

Systematically hydrolyse the protein chain and identify each amino acid

25
Q

How do you separate amino acids

A

TLC or paper chromatography

26
Q

What is a proteins secondary structure caused by

A

Caused by hydrogen bonding between the N-H and the C=O groups of the peptide links along the protein chain causing alpha helix and beta pleated sheets

27
Q

Define alpha helix

A

Hydrogen bonds formed every four amino acids forcing the chain into a cylindrical formation. Elastic and flexible.

28
Q

Define beta pleated sheets

A

Parallel regions of the protein line up allowing hydrogen bonds to form between them, leading to a flat sheet like structure.

29
Q

Where do you find beta pleated sheet proteins

A

In association with Alzheimer’s

30
Q

Define tertiary structure

A

The overall 3D shape of a protein. Maintained by hydrogen bonds, ionic interactions and disulphides bonds between R groups of amino acids

31
Q

What is the tertiary structure necessary for

A

Biochemical activity

32
Q

What is broken when a protein is denatured

A

Tertiary structure

33
Q

What are disulphides bonds

A

Between two -SH variable groups. Form strong S-S bonds

34
Q

How can sulphide bonds be broken

A

They are destroyed by heat, reduction or reaction with a base

35
Q

Define enzyme

A

Proteins that act as biological catalysts, providing an alternative reactions of lower Eact

36
Q

How do enzymes works

A

Substrates bond in an active site.

37
Q

Define lock and key hypothesis

A

Only molecules that have the right shape can fit into the active site

38
Q

What determines how a substrate will bind

A

The size and orientation of an amino acid

39
Q

How does a substrate bind to the active site

A

Hydrogen bonding, ionic bonding, and van der waals forces

40
Q

What does a stereospecific active site cause

A

An active site which bonds to only one enantiomer of a racemate

41
Q

Define enzyme inhibitor

A

A molecule that binds to an enzyme active site and decrease its activity is called an enzyme inhibitor

Chemistry (24 decks)

Brainscape helps you reach your goals faster, through stronger study habits.
© 2024 Bold Learning Solutions. Terms and Conditions