Proteins Flashcards

1
Q

molecules w/ elongated shape & one dimension much longer

A

Fibrous Proteins

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2
Q

structure of fibrous proteins

A

Linear and form aggregate to form macromolecular structure

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3
Q

peptide chains folded into spherical or globule shapes

A

Globular Proteins

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4
Q

structure of globular proteins

A

Hydrophilic side chains on outside; hydrophobic in interior

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5
Q

found associated with a membrane system of a cell; opposite of globular protein

A

Membrane Proteins

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6
Q

fibrous vs. globular: water

A

fibrous - water soluble

globular - dissolve in water

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7
Q

Fibrous vs. globular: secondary structure

A

Fibrous - single type

Globular - several types

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8
Q

Fibrous vs. globular: function

A

Fibrous - support and external protection

Globular - involved in metabolism, transport, regulation, catalysis

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9
Q

5 fibrous proteins

A

Keratin, collagen, elastin, myosin, fibrin

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10
Q

Found in wool, feathers, hooves, silk, and nails

A

Keratin

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11
Q

Found in tendons, bones, and other connective tissues

A

Collagen

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12
Q

Found in blood vessels

A

Elastin

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13
Q

Found in muscle tissue

A

Myosin

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14
Q

Found in blood clots

A

Fibrin

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15
Q

5 common globular proteins

A

Insulin, myoglobin, hemoglobin, transferrin, immunoglobulins

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16
Q

Regulatory hormone for controlling glucose metabolism

A

Insulin

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17
Q

Involved in oxygen storage in muscles

A

Myoglobin

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18
Q

Involved in oxygen transport in blood

A

Hemoglobin

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19
Q

Involved in iron transport in blood

A

Transferrin

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20
Q

Involved in immune system responses

A

Immunoglobulins

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21
Q

Why are we able to remove lipids or cholesterols in the body?

A

Because they are bound with proteins which makes it easier to transport

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22
Q

Keratin structure

A

Coiling @ higher levels produce strength, intercoil disulfide bridge

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23
Q

Collagen

A

most abundant of all proteins in humans (30% of total body protein)

24
Q

Characteristics of collagen

A

Rich proline content = triple helix conformation; form fibrils with cross linking on helices; stiffening of skin associated with aging

25
Q

Predominant structure of collagen

A

Triple helix
Forms like a rope
Presence of glycine and proline

26
Q

Structure of hemoglobin

A
  • Tetramer (four peptide chains each contain heme group = binds to O2)
  • Iron atom @ center interact w/ O2 ; 1 hemoglobin: 4 O2 molecules
27
Q

Structure of myoglobin

A
  • Single peptide chain & a heme unit hence carry one O2

- Higher affinity for O2 than hemoglobin; working muscles

28
Q

Role of biochemical catalysts = enzymes

A

Catalytic proteins

29
Q

immunoglobulins or antibodies function in immune

system

A

Defense proteins

30
Q

Bind to small biomolecules and transport e.g. hemoglobin

A

Transport proteins

31
Q

transmit signals to coordinate biochemical processes between different cells, tissues, and organ ex. Hormones

A

Messenger proteins

32
Q

Necessary for movement. Filament like proteins in muscles, flagella of sperm

A

Contractile proteins

33
Q

Stiffness and rigidity ex. Collagen & keratin

A

Structural proteins

34
Q

@ cell membrane and control movement

A

Transmembrane proteins

35
Q

Bind & store molecules for future use ex ferritin

A

Storage proteins

36
Q

Important in early stages of life e.g casein in milk

A

Nutrient proteins

37
Q

Site of binding for messenger proteins & enact function

A

Regulatory proteins

38
Q

Necessary for movement. Filament like proteins in muscles, flagella of sperm

A

Contractile proteins

39
Q

Maintain fluid balance between blood & tissue; e.g. albumin and globulin in capillary beds

A

Fluid-balance proteins

40
Q

conjugated proteins that contain carbohydrates or carbohydrate derivatives in addition to amino acids

A

Glycoproteins

41
Q

Collagen in glycoproteins

A
  • attached sugar units by glycosidic linkages; related to cross linking
  • Direct assembly of helices into complex aggregations = collagen fibrils
42
Q

glycoprotein as a protective response to the invasion of microorganisms or foreign molecules; antigen = foreign substance vs. antibody

A

Immunoglobulin

43
Q
  • Conjugated proteins that are composed of both lipids and amino acids
  • classified according to their density
A

Lipoproteins

44
Q

involved in the transport system for lipids in the bloodstream

A

Plasma lipoprotein

45
Q

Four major classes of plasma lipoprotein

A

Chylomicrons
Very-low-density lipoproteins
Low-density lipoproteins
High-density lipoproteins

46
Q

transport dietary triacylglycerols from the intestine to the liver and to adipose tissue

A

Chylomicrons

47
Q

Transport triacylglycerols synthesized in the liver to adipose tissue

A

Very-low-density lipoproteins (VLDL)

48
Q

transport cholesterol synthesized in the liver to cells throughout the body

A

Low-density lipoproteins (LDL)

49
Q

collect excess cholesterol from body tissues and transport it back to the liver for degradation to bile acids

A

High-density lipoproteins

50
Q

Blood proteins that contain iron

A

Ferritin

51
Q

Thick yellow secretion; high antibodies; more carbo

A

Colostrum

52
Q

Protection in the cell membrane

A

Phospholipids

53
Q

Free cholesterol content

A

Cystotoxic = contains toxic contents

54
Q

Protective form of storage of the cell; helps transport plasma lipoprotein to other tissues and organs

A

Cholesterol esters

55
Q

Excellent long term energy storage in the molecules made up of glycerol

A

Triglycerides

56
Q

How to remove free cholesterol?

A

Bind with amino acids to easily transport to the liver which will be cleared and become a good cholesterol