Brainscape's Knowledge GenomeTM

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


See full index

Bio-chem > Protiens > Flashcards

Protiens Flashcards

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

what does organic mean?

A

Containing carbon

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

what are the roles of protiens

A

-structural
-metabolic
-transport

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

what elements do amino acids contain

A

carbon, hydrogen, oxygen, nitrogen and sometimes sulphur and phosphate

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

Polymer of amino acid

A

Polypeptide

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

Carboxyl/acid group

A

c=0
-oh

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

amino group

A

N-h
-h

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

What’s an R group

A

-variable group

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

how many amino acids are there?

A

20, 8 essential ones

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

what does essential mean

A

must get them in our diet

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

properties of amino acids

A

-they’re soluble
-they’re amphoteric

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

how amino acids differ

A

-size
-polarity
-charge

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

what are the positive and negative amino acids called

A

positive- base
negative- acid

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

how do amino acids join together

A

join by a reaction between amino group of one protein and carboxyl group of the other amino acid
-this is a condensation reaction

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

bond/link between amino acids

A

peptide link/bonds

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

similarity and difference between glyosidic bond and peptide bond

A

similarity- condensation build up and hydrolysis breaks down
difference- peptide has link between C-N and glyosidic bond between
C-O-C

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

amphoteric

A

amino group accepts H+ ions and carboxylic group donates H+ ions
-in acidic environment, amine accepts H+
-in alkaline environment, carboxyl/acid group donates H+

17
Q

primary structure

A

specific sequence of amino aicds- one long chain, coded by the DNA of the cell

18
Q

secondary structure

A

form when polypeptide chain takes up a particular shape through folding

19
Q

forms of secondary structure

A

alpha helix and beta sheet

20
Q

how is alpha helix and beta pleated sheet formed

A

hydrogen bonds between hydrogen of amine and oxygen of carboxyl

21
Q

tertiary structure

A

secondary structure folded further to form complex shape due to 4 different bonds between acids

22
Q

4 types of bond in tertiary protiens

A

Disulphide, ionic, hydrogen, hydrophilic/phobic interactions

23
Q

hydrogen bonds

A

form between hydrogen atoms with slight positive charge and other atoms with a slight negative charge
-amino and carboxyl group
-give protein strength

24
Q

ionic bonds

A

between carboxyl and amino groups that are part of R groups, positive and negative groups strongly attracted to each other

25
Q

disulphide links

A

-the R group of amino acid cysteine contains sulphur
-disulphide bridges formed between the R groups of two cysteines, strong covalent bonds

26
Q

hydrophobic and hydrophilic interactions

A

-hydrophobic parts of R groups associate together in centre of polypeptide in water (rotate inwards)
-hydrophilic parts associate with each other on the edge of the polypeptide to be close to water (turn outwards)

27
Q

quaternary structure

A

more than one polypeptide chain, arranged in a complex structure

28
Q

example of quaternary protein and its structure

A

Haemoglobin, contains the haem group which bonds to the o2 and polypeptide chains

29
Q

strong to weakest bonds

A

ionic, disulphide, hydrogen

30
Q

properties of fiberous proteins

A

-mostly insoluble
-not folded into a complex 3D shape
-strong, long molecules
-have high proportion of amino acids with hydrophobic R groups
-repetative AA sequence in primary structure creates organised structure, compact

31
Q

properties of globular proteins

A

-folded to keep hydrophobic R groups inside and hydrophillic R groups outside
-soluble in water
-spherical in shape
-must be soluble for processes such as chemical reactions, immunity and muscle contraction

32
Q

example of globular protein

A

insulin- transported in blood so must be soluble

33
Q

example of fiberous protein

A

-keratin and elastin

34
Q

structure of heamaglobin

A

globular, quaternary protein with 4 subunits, 2 alpha globin and 2 beta globin chains-
each subunit has one haem that has iron which binds to oxygen

35
Q

denaturisation of proteins

A

-typically effect secondary , tertiary or quintenary structures but doesn’t affect peptide bonds in primary structure

Bio-chem (12 decks)

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