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Biochemistry > proteins<3 > Flashcards

proteins<3 Flashcards

1
Q

name the 4 structural levels in proteins

A

PRIMARY -> sequence of amino acids
SECONDARY -> alpha helicase and beta pleated sheets
TERTIARY -> bonding between alpha helices and beta sheets
QUATERNATARY -> further internal and external bonding

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2
Q

describe primary structure

A

simple sequence of amino acids in chain.
the most simple description of protein structure
N terminus and C terminus

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3
Q

describe secondary structure ALPHA HELICASE!

A

can be R or L handed - usually R
proteins vary in alpha heliacse length and content
ampiphathic helicase -hydrphillic outward hydrophobic inward

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4
Q

describe secondary structure BETA STRANDS AND SHEETS

A

almost fully extended sections of polypeptide
not as compact as helicase
strands can be parallel or antiparallel
parallel is less stable

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5
Q

how are beta sheets stabalised?

A

by H bonds between carbonyl oxygen and amide hydrogen on adjacent strand

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6
Q

describe tertiary protein structure

A

Amino acids come closer together in tertiary level
resulting side chain interactions
stabilised by non covalent interactions between side chains covalent disulphide bridges also present

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7
Q

describe tertiary structure SUPER SECONDARY

A

also called MOTIFS - combination of alpha helices and beta strands + loops
motifs can be linked to specific protein functions
examples- coiled-coiled, hairpin, greek key

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8
Q

describe tertiary structure DOMAINS

A

compact units and indépendant of each other but joined at primary structures
each domain consist of several elements of secondary structures
can group proteins with simular sequences and domains
direct relationship between domain and structure

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9
Q

describe quaternary structure

A

further level of structure seen in many proteins not all!
refers to subsist which have independent polypeptide chain
stabilised with weak non covalent bonds, hydrophobic interactions with electrostatic forces contributing

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10
Q

where do salt bridges form in protein

A

deep inside hydrophobic part

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11
Q

what is a denaturant required to do?

A

unfold Native (N) form of protein

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12
Q

chemical, heat and pressure denaturant all work by?

A

causing disruption of bond interaction

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13
Q

name three types of denaturant?

A

pressure
chemical
heat

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14
Q

do denatured proteins still have a lot of internal structure

A

yes

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15
Q

can all proteins renature spontaniously

A

NO

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16
Q

does denaturation require more or less energy compared to renaturation?

A

LESS

17
Q

how do proteins fold?

A

spotaniously to achieve lowest energy state

18
Q

do enzymatic pathways have weak or strong interactions?

A

WEAK

19
Q

key features of WANDERWAAL forces

A

short range, small magnitude,
only when atoms in close proximity,
dipolar
clusters add strength

20
Q

what is Ka

A

association constant

21
Q

how do we work out Ka

A

Ka =1/Kd

22
Q

name 4 further side chain modifications

A

hydroxlation,
glycosylation,
phosphorolation,
collagen

23
Q

what do hydroxylation do?

A

add OH

24
Q

what does glycosylation do?

A

add sugar chains

25
Q

what does phosphorlation do?

A

add phosphate

26
Q

give key features of hydroxylation

A

occurs immediately after amino acid chain completed
found in collagen
requires vitamin C.

27
Q

key features of glycosylation

A

occurs immediately after amino acids chain completed
found mainly in secreted proteins & in those located on surface of cells
used for stabalisation of protein structure

28
Q

phophorolation key features

A

reversible
occur many times in life of protein
control of enzyme activity

29
Q

collagen key features

A

protein of connective tissue
can take many forms depending on requirements
eg, tendons-> like rope
in skin-> loosely woven allowing expansion

30
Q

what are myoglobin and heamoglobyn?

A

globular proteins

31
Q

what structures does myoglobin have?

A

primary, secondary and tertiary

32
Q

what is myoglobyn

A

one polypeptide chain folded up into globule

33
Q

what does heamoglobyn comprise of?

A

the equivelent of 4 myoglobin molecules

34
Q

does haemoglobin have quaternary structures?

A

YES

Biochemistry (12 decks)

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