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BIOCHEM > UNIT 4- PROTEINS > Flashcards

UNIT 4- PROTEINS Flashcards

1
Q

what is a domain and how many types are there?

A

domain is compact folded regions of TERIARY STRUCTURE

-2types= structural + functional

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2
Q

native state?

A

most stable folding + function of protein

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3
Q

consequence of misfolding?

A

loss of normal protein= disorded twisted aggregates

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4
Q
  1. denaturation reversible?
A

can be reversed if agent is weak, if non rev=NONSOLUBLE-> FIBROUS

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5
Q

is folding reversible ?

A

yes

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6
Q

which are the globular proteins? 2

A
  1. HEMOGLOBIN

2. IMMUNOGLOBIN

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7
Q

which are the Fibrous proteins? 3

A
  1. collagen
  2. keratin
  3. fibroin
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8
Q

solubility + branching of globular proteins?

A

SOLUBLE + COMPACT

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9
Q

solubility + branching of fibrous proteins?

A

INSOLUBLE + EXTENDED

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10
Q

2ndry structure of globular proteins?

A

a-helix, b sheets + loop structures

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11
Q

2ndry structure of fibrous proteins?

A

a helix beta sheets

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12
Q

4th structure of globular proteins?

A

held by non covalent forces

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13
Q

4th structure of of fibrous proteins?

A

held by covalent disulphide bridges

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14
Q

functions of globular proteins?

A

metabolism, enzymes, trnapsort, immunity

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15
Q

functions of of fibrous proteins?

A

structure of body, tendons, muscles, ligaments

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16
Q

shape of globular proteins?

A

spherical phobic inside

+ phiic outside e.g MICELLES, MYOGLOBIN

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17
Q

shape of fibrous proteins?

A

rodlike

18
Q

what is keratin made of? (a keratin)

A

RIGHT HANDED a helix

a helix>protofilament>protofibril

19
Q

where is keratin found?

A

hair, skin, nails hooves

20
Q

what is fibroin made of?

A

antiparallel b sheets GLY on 1 face ALA on next

21
Q

how is fibroin stabilised by?

A

H BONDS + VDW

22
Q

COLLAGEN 1 what is it made of?

A

3x pp chain of GLY-POLINE-5HYDROXYPROLINE

-monomer = tropocollagen (v strong extended)

23
Q

what is collagen 1s 2ndry structure?

A

3ppc= left handed helix each chain HBOND eachother =strength

-RIGHT HANDED TWIST

24
Q

over view of collagen formation? 4

A

=procollagen = triple helix GLY-PRO-5HYDROXYPRO

  • tropcollagen= maturation of triple helix
  • fibrils=tropocollagen linearly crosslinked via CB
  • fibres= fibrils side by side
25
Q

how do human genetic defetcs happen?

A

replacement of GLY with CYS/SER (bigger R group)

26
Q

what is EDS (EHLERS DANLOS SYNDROME ?

A

stretchy bruisable skin

-mutation affecting assembly of collagen FIBERS

27
Q

what Is OSTEOGENESIS IMPERFECTA?

A

mutation in collagen 1 = bone fractures

28
Q

what is dentiogenesis imperfecta?

A

blue/grey yellow due to changes in collagen in dentin

29
Q

scurvy?

A

lack of vit c = lesions on skin + gums, weakening of bvs

30
Q

what is the heteroprotein haemoglobin made of?

A

2 a and 2 b ppc

-each ppc has heme group

31
Q

how does haemoglobin act as a buffer?

A

histidine binds to fe2+

32
Q

tertiary structure of haemoglobin?

A

like micelle

-open top hydrophobic cleft to protect fe2+ from oxidation

33
Q

quaternanary structure of haemoglobin?

A

low affintity = T tense
high affinity = R relaxed
-T>R cooperative effect when 02 binds to fe2+ and pka decreases
-4 binding sites

34
Q

IMMUNOGLOBULINS where is it synthesised?

A

b lymphocytes

35
Q

IMMUNOGLOBULIN primary structure?

A

4 ppc = 2 light chains 2 heavy joined via disulphide bridges
light chains = NON GLYCOSILIATED
heavy chains = GLYCOSILIATED

36
Q

IMMUNOGLOBULIN secondary structure?

A

b sheet ahelix

-antigen binding ssite and variable region

37
Q

what are the N TERMINAL ENDS for IMMUNOGLOBULIN ?

A

highly variable + responsible for specifity

38
Q

function of insulin receptor?

A

regulate cel differentiation, growth, metabolism og glucose

39
Q

primary structure and secondary structure of insulin?

A

4ppc = 2 a subunits 2 b subunits linked by disulphide bridges
-a helix beta sheets

40
Q

teriary structure of insulin?

A
  1. LIGAND BINDING DOMAIN = for insulin located in EXTRACELL of a chain
  2. CATALYTIC DOMAIN = in CYTOSOLIC comp of B chain (ATP+3 TYROSINE)
41
Q

QUATERNARY STRCUTURE OF INSULIN?

A
  1. INACTIVE RECETOR = MONOMER= BINDS INSLULIN WITH LOW AFFINITY
  2. ACTIVE RECEPTOR = DIMER =HIGH AFFINITY insulin binding + stimulated kinase activity
42
Q

what does INSULIN belong to and do?

A

belongs to the Tyrosine Kinase Receptor. which binds insulin via dephosphorylation

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