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BIOCHEM > UNIT 4- PROTEINS > Flashcards

UNIT 4- PROTEINS Flashcards

(42 cards)

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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?

18
Q

what is keratin made of? (a keratin)

Study These Flashcards
A

RIGHT HANDED a helix

a helix>protofilament>protofibril

19
Q

where is keratin found?

Study These Flashcards
A

hair, skin, nails hooves

20
Q

what is fibroin made of?

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A

antiparallel b sheets GLY on 1 face ALA on next

21
Q

how is fibroin stabilised by?

Study These Flashcards
A

H BONDS + VDW

22
Q

COLLAGEN 1 what is it made of?

Study These Flashcards
A

3x pp chain of GLY-POLINE-5HYDROXYPROLINE

-monomer = tropocollagen (v strong extended)

23
Q

what is collagen 1s 2ndry structure?

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A

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

-RIGHT HANDED TWIST

24
Q

over view of collagen formation? 4

Study These Flashcards
A

=procollagen = triple helix GLY-PRO-5HYDROXYPRO

  • tropcollagen= maturation of triple helix
  • fibrils=tropocollagen linearly crosslinked via CB
  • fibres= fibrils side by side
25
how do human genetic defetcs happen?
replacement of GLY with CYS/SER (bigger R group)
26
what is EDS (EHLERS DANLOS SYNDROME ?
stretchy bruisable skin | -mutation affecting assembly of collagen FIBERS
27
what Is OSTEOGENESIS IMPERFECTA?
mutation in collagen 1 = bone fractures
28
what is dentiogenesis imperfecta?
blue/grey yellow due to changes in collagen in dentin
29
scurvy?
lack of vit c = lesions on skin + gums, weakening of bvs
30
what is the heteroprotein haemoglobin made of?
2 a and 2 b ppc | -each ppc has heme group
31
how does haemoglobin act as a buffer?
histidine binds to fe2+
32
tertiary structure of haemoglobin?
like micelle | -open top hydrophobic cleft to protect fe2+ from oxidation
33
quaternanary structure of haemoglobin?
low affintity = T tense high affinity = R relaxed -T>R cooperative effect when 02 binds to fe2+ and pka decreases -4 binding sites
34
IMMUNOGLOBULINS where is it synthesised?
b lymphocytes
35
IMMUNOGLOBULIN primary structure?
4 ppc = 2 light chains 2 heavy joined via disulphide bridges light chains = NON GLYCOSILIATED heavy chains = GLYCOSILIATED
36
IMMUNOGLOBULIN secondary structure?
b sheet ahelix | -antigen binding ssite and variable region
37
what are the N TERMINAL ENDS for IMMUNOGLOBULIN ?
highly variable + responsible for specifity
38
function of insulin receptor?
regulate cel differentiation, growth, metabolism og glucose
39
primary structure and secondary structure of insulin?
4ppc = 2 a subunits 2 b subunits linked by disulphide bridges -a helix beta sheets
40
teriary structure of insulin?
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
QUATERNARY STRCUTURE OF INSULIN?
1. INACTIVE RECETOR = MONOMER= BINDS INSLULIN WITH LOW AFFINITY 2. ACTIVE RECEPTOR = DIMER =HIGH AFFINITY insulin binding + stimulated kinase activity
42
what does INSULIN belong to and do?
belongs to the Tyrosine Kinase Receptor. which binds insulin via dephosphorylation

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