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Biochemistry > Protein Structure and Function > Flashcards

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
Proteins that undergo ATP independent degradation
Extracellular proteins Membrane-association proteins Long-lived intracellular proteins SITE: LYSOSOMES i.e. blood glycoprotein
26
Proteins that undergo ATP dependent degradation
Regulatory proteins with short half lives Abnormal or misfolded proteins SITE: cytosol requires UBIQUITIN
27
Key molecule in protein degradation Highly conserved protein
UBIQUITIN
28
Ubiquinated proteins are degraded in
Proteosome - located in the CYTOSOL
29
Proteosome Inhibitor Used in Multiple Myeloma For Hepatocellular Carcinoma
Bortezomib
30
Maintain the colloid osmotic pressure of the plasma
ALBUMIN
31
Most abundant PLASMA PROTEIN
ALBUMIN
32
LEAST abundant PLASMA PROTEIN
alpha 1 globulin
33
Plasma protein with FASTEST electrophoretic mobility
PREALBUMIN (transthyretin)
34
Most plasma proteins are synthesized in the LIVER EXCEPT
Immunoglobulins - plasma cells
35
Most plasma proteins are glycoproteins EXCEPT
Albumin - simple protein
36
Plasma proteins that exhibit POLYMORHISM
``` a1 antitrypsin haptoglobin transferrin ceruloplasmin immunoglobulins ```
37
Group of Plasma proteins whose concentration increases or decreases in response to inflammatory and neoplastic conditions
ACUTE PHASE REACTANTS
38
Positive Acute Phase Reactants concentration increases in response to inflammatory and neoplastic conditions
``` CRP Ceruloplasmin Haptoglobulin Fibrinogen alpha 1 acid glycoproteun alpha 1 antiprotease ```
39
Properties of proteins at ISOELECTRIC pH
``` they have NO net charge they do NOT have eletrophoretic mobility maximum precipitability maximum solubility minimum buffering action ```
40
Polypeptide formation in amino acid is by
PRIMARY STRUCTURE
41
Confirmatory test for proteins
Western Blot ELISA Chip assay Dot blot
42
2 Important Phosphoproteins
CASEIN (milk) | OVOVITELLIN ( egg yolk)
43
An alpha helix of a protein is most likely be disrupted if a missense mutation introduces the ff AA within the alpha helical structure
GLYCINE
44
Molecules up to size 4 KD is identified by
Quadrupole Mass Spectrometry
45
Major collagen present in HYPERTROPHIC CARTILAGE
Type X
46
Major collagen in KELOID
Type 3 > Type 1
47
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
FIBROUS
48
Quarter arrangement is seen jn
COLLAGEN
49
Type of collagen present in SKIN HEMIDESMOSOMES
Type XVII
50
Type of collagen present in RHABDOMYOSARCOMA
Type XIX
51
Type of collagen present in BRAIN
Type XXV
52
Type of collagen present in TESTIS AND OVARY
Type XXVI
53
Functions of Golgi Bodies
O-glycosylation of proteins protein sorting processing of oligosaccharide chains of glycoproteins
54
Prion Related Protein Diseases
``` Alzheimer Disease Parkinson's Disease Huntington's Disease Fronto Temporal Dementia Dementia with Lewy Bodies Amyloidosis Beta thalassemia ```
55
Which of the ff groups of proteins assist in the folding of other proteins? a. Proteases b. Proteosomes c. Templates. d. Chaperones
d. Chaperones
56
Chaperones
Belong to heat shock proteins wide range of expression present from bacteria to human also known as STRESS PROTEINS

Biochemistry (75 decks)

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