Protein Structure and Function Flashcards

1
Q

Specialized group of proteins required for the PROPER FOLDING OF MANY SPECIES OF PROTEINS

Prevents aggregation and misfolding

A

Chaperones

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2
Q

Due to UNFOLDING AND DISORGANIZATION OF A PROTEIN

A

Denaturation

does NOT affect primary structure

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3
Q

Globular Proteins

hemoglobin
myoglobin
albumin
globulin
most enzymes
A

spherical
MORE soluble
has DYNAMIC functions

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4
Q

Fibrous Proteins

collagen fibers
elastin fibers
keratin

A

elongated or needle shaped
MINIMALLY soluble
STRUCTURAL proteins

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5
Q

Most abundant protein in the body

A

Collagen

3 polypeptides (alpha-chains) wound around in triple helix formation (stabilized by hydrogen bonds)

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6
Q

MC form of collagen

A

Type 1 collagen

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7
Q

Usual pattern of AA in collagen

A

Gly - glycine
X - proline
Y - hydroxyproline, hydroxylysine

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8
Q

Type I collagen

A

BONE

OI

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9
Q

Type 2 collagen

A

Cartilage

Achondrogenesis type II

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10
Q

Type 3 collagen

A

Reticulin fibers, blood vessels, granulation tissue

Ehlers Danlos (vascular type)
aortic rupture, aortic aneurysms
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11
Q

Type 4 collagen

A

Basement Membrane

Alport Syndrome
Goodpasture Syndrome

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12
Q

Type 5 collagen

A

bone, skin, fetal tissues, placenta

Ehler Danlos (classical type)

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13
Q

Type 7 collagen

A

Anchoring fibrils

Dystrophic epidermolysis bullosa

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14
Q

Connective tissue with rubber like properties allowing extensibility and elastic recoil

A

Elastin

non hydroxylated PROLINE, LYSINE - major AA

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15
Q

Scaffold for the synthesis of elastin fibers

A

FIBRILLIN

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16
Q

Cross links precursor tropoelastin together

A

DESMOSINE

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17
Q

Defective in Marfan Syndrome

skeletal change
aortic dissection
ectopic lentis (upward, outward)
A

Fibrillin

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18
Q

Triad of Marfan’s Syndrome

A

Skeletal changes
Ectopic lentis - upward and temporal subluxatiob
aortic aneurysm

FIBRILLIN 1

zonular fibers in the lens
periosteum
aorta

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19
Q

International Criteria to classify Marfan syndrome

A

Ghent Criteria

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20
Q

Mutation in TGR Beta Receptors

Characterized by aortic aneurysms, cleft palate, hypertelorism

A

Loeys-Dietz

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21
Q

Alpha helix coiled structure wind arpund each other to form a super helix

Rich in HYDROPHOBIC AA - Ala, Leu, Met, Val, Phe

A

KERATIN

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22
Q

Major protein component of Renal Glomerular and other Basal Laminas

A

LAMININ

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23
Q

Glycosaminoglycans present in BASAL LAMINA

A

Heparin

Heparan sulphate

24
Q

2 types of Protein Degradation

A

ATP Independent Degradation

ATP Dependent Degradation

25
Q

Proteins that undergo ATP independent degradation

A

Extracellular proteins
Membrane-association proteins
Long-lived intracellular proteins

SITE: LYSOSOMES

i.e. blood glycoprotein

26
Q

Proteins that undergo ATP dependent degradation

A

Regulatory proteins with short half lives
Abnormal or misfolded proteins

SITE: cytosol

requires UBIQUITIN

27
Q

Key molecule in protein degradation

Highly conserved protein

A

UBIQUITIN

28
Q

Ubiquinated proteins are degraded in

A

Proteosome - located in the CYTOSOL

29
Q

Proteosome Inhibitor

Used in Multiple Myeloma

For Hepatocellular Carcinoma

A

Bortezomib

30
Q

Maintain the colloid osmotic pressure of the plasma

A

ALBUMIN

31
Q

Most abundant PLASMA PROTEIN

A

ALBUMIN

32
Q

LEAST abundant PLASMA PROTEIN

A

alpha 1 globulin

33
Q

Plasma protein with FASTEST electrophoretic mobility

A

PREALBUMIN (transthyretin)

34
Q

Most plasma proteins are synthesized in the LIVER EXCEPT

A

Immunoglobulins - plasma cells

35
Q

Most plasma proteins are glycoproteins EXCEPT

A

Albumin - simple protein

36
Q

Plasma proteins that exhibit POLYMORHISM

A
a1 antitrypsin
haptoglobin
transferrin
ceruloplasmin
immunoglobulins
37
Q

Group of Plasma proteins whose concentration increases or decreases in response to inflammatory and neoplastic conditions

A

ACUTE PHASE REACTANTS

38
Q

Positive Acute Phase Reactants

concentration increases in response to inflammatory and neoplastic conditions

A
CRP
Ceruloplasmin
Haptoglobulin
Fibrinogen
alpha 1 acid glycoproteun
alpha 1 antiprotease
39
Q

Properties of proteins at ISOELECTRIC pH

A
they have NO net charge
they do NOT have eletrophoretic mobility
maximum precipitability
maximum solubility
minimum buffering action
40
Q

Polypeptide formation in amino acid is by

A

PRIMARY STRUCTURE

41
Q

Confirmatory test for proteins

A

Western Blot
ELISA
Chip assay
Dot blot

42
Q

2 Important Phosphoproteins

A

CASEIN (milk)

OVOVITELLIN ( egg yolk)

43
Q

An alpha helix of a protein is most likely be disrupted if a missense mutation introduces the ff AA within the alpha helical structure

A

GLYCINE

44
Q

Molecules up to size 4 KD is identified by

A

Quadrupole Mass Spectrometry

45
Q

Major collagen present in HYPERTROPHIC CARTILAGE

A

Type X

46
Q

Major collagen in KELOID

A

Type 3 > Type 1

47
Q

The structural proteins are involved in maintaining the shape of a cell or in the formation of matrices in the body. The shape of these protein is

A

FIBROUS

48
Q

Quarter arrangement is seen jn

A

COLLAGEN

49
Q

Type of collagen present in SKIN HEMIDESMOSOMES

A

Type XVII

50
Q

Type of collagen present in RHABDOMYOSARCOMA

A

Type XIX

51
Q

Type of collagen present in BRAIN

A

Type XXV

52
Q

Type of collagen present in TESTIS AND OVARY

A

Type XXVI

53
Q

Functions of Golgi Bodies

A

O-glycosylation of proteins
protein sorting
processing of oligosaccharide chains of glycoproteins

54
Q

Prion Related Protein Diseases

A
Alzheimer Disease
Parkinson's Disease
Huntington's Disease
Fronto Temporal Dementia
Dementia with Lewy Bodies
Amyloidosis
Beta thalassemia
55
Q

Which of the ff groups of proteins assist in the folding of other proteins?

a. Proteases
b. Proteosomes
c. Templates.
d. Chaperones

A

d. Chaperones

56
Q

Chaperones

A

Belong to heat shock proteins
wide range of expression
present from bacteria to human
also known as STRESS PROTEINS