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BIO 024: Biochemistry > Proteins II > Flashcards

Proteins II Flashcards

1
Q

It is a peptide chain twists into a spiral.

A

a-helix

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2
Q

It is two or more peptide chains, called strands lined up side-by-side.

A

B-pleated sheet

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3
Q

Reverses the direction of a polypeptide chain, helping it form a compact, globular shape. It is stabilized by the formation of hydrogen and ionic bonds.

A

B-bends

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4
Q

Bond in which amino acids with positively and negatively charged side chains attract each other

A

Ionic bond

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5
Q

Results in the unfolding and disorganization of the protein’s secondary and tertiary structures, which are not accompanied by hydrolysis of peptide bonds.

A

Protein denaturation

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6
Q

Is a protein in which only one peptide chain is present.

A

Monomeric protein

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7
Q

Is a protein in which more than one peptide chain is present. The peptide chains present are called protein subunits.

A

Multimeric protein

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8
Q

Is a protein in which only amino acid residues are present.

A

Simple protein

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9
Q

Is a protein that has one or more non-amino acid entities present in its structure in addition to one or more peptide chains.

A

Conjugated Protein

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10
Q

These include substances formed from simple conjugated proteins.

A

Derived protein

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11
Q

It is a non-amino acid group present in a conjugated protein. These non-amino acid components, which may be organic or non-organic.

A

Prosthetic group

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12
Q

Identify what type of Conjugated protein:

Ribosomes (site for protein synthesis in cells)
Viruses (self-replicating, infectious complex)
Chromatin
Products from glandular tissues
Germs of grains

A

Nucleoproteins

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13
Q

Identify what type of Conjugated protein:

Mucin aka mucoproteins - more carbs less proteins (saliva, mucous secretion of the nose)
Tendomucoid (tendons)
Osseomucoid (bones)
gamma globulin (antibody)
Interferon (antiviral protection)
Simple proteins like globulins and albumins

A

Glycoproteins

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14
Q

Identify what type of Conjugated protein:

Casein (milk)
Vitellin (egg yolk

A

Phosphoproteins

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15
Q

Identify what type of Conjugated protein:

Hemoglobin (blood -carrier of O2 in blood )
Myoglobin (oxygen binder in muscles)
Cytochromes
Rhodopsin

A

Chromoproteins/Hemoproteins

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16
Q

Identify what type of Conjugated protein:

Lecithin
Cephalin
low-density lipoprotein (LDL) – lipid carrier
high-density lipoprotein (HDL) – lipid carrier

A

Lipoproteins

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17
Q

Identify what type of Conjugated protein:

iron–ferritin (storage complex for iron)
zinc–alcohol dehydrogenase (enzyme in alcohol oxidation)

A

Metalloproteins

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18
Q

proteins which have undergone slight intramolecular rearrangement through the hydrolytic action of certain physical and chemical agents. Synonymous w/ denatured proteins.

A

Primary Protein Derivatives

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19
Q

Identify what type of Conjugated protein:

-Serum albumin (blood)
-Lactalbumin (milk)
-Ovalbumin (eggwhite)

A

ALBUMINS

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20
Q

Identify what type of Conjugated protein:

-Ovoglobulin (eggwhite),
-Edestin (hempseed),
-Legumin (peas)
-Myosinogen (muscles)
-Serum globulin (blood)

A

GLOBULINS

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21
Q

Identify what type of Conjugated protein:

-Glutenin (wheat)
-Oryzenin (rice)

A

GLUTELINS

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22
Q

Identify what type of Conjugated protein:

-Gliadin (wheat)
-Zein (corn)
-Hordein (barley)

A

PROLAMINES

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23
Q

Identify what type of Conjugated protein:

–Thymus histones
-Scobrone of Mackerel

A

HISTONES

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24
Q

Identify what type of Conjugated protein:

Salmin (salmon sperm)

A

PROTAMINES

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25
Q

Identify what type of Conjugated protein:

-Keratin (epidermal tissues)
-Elastins (Ligaments)
-Collagen (hides, bones and cartillage)

A

SCLEROPROTEINS (Albuminoids)

26
Q

It is the product of more extensive hydrolysis, mixtures of fragments of original proteins varying in composition and size, and exhibit certain common properties such as solubility in water and non-coagulability by heat.

A

Secondary Protein derivatives

27
Q

Soluble in water, precipitated by conc.HNO3 and by half saturation with
(NH4)2SO4 or ZnSO4. Not coagulated by heat

A

PRIMARY PROTEOSES

27
Q

Soluble in water, precipitated by conc.HNO3 and by half saturation with
(NH4)2SO4 or ZnSO4. Not coagulated by heat

A

PRIMARY PROTEOSES

28
Q

Precipitated only by complete saturation with (NH4)2SO4 but nit with picric acid and HNO3

A

SECONDARY PROTEOSES

29
Q
  • Soluble in water
  • Not coagulated by heat
  • Not precipitated by saturation with (NH4)2SO4 but by certain alkaloidal reagents, such as phosphotingstic and tannic acids.
A

PEPTONES

30
Q

Are combinations of two or more amino acids, the carboxyl group of one being united with the amino group of the other. Present properties like peptones
Ex. di, tri,tera,penta etc.

A

PEPTIDES

31
Q

Protein whose molecules have an elongated shape with one dimension much longer than the others.

Properties:
*Tend to have simple, regular and linear structures.
*Largely insoluble in ordinary aqueous media
*Molecular weights are high
*Functions is for structural and support

A

FIBROUS

32
Q

molecules have peptide chains that are folded into spherical or globular shapes .The folding in such that most of amino acids with hydrophobic side chains (nonpolar R groups) are in the interior of the molecules and most of the hydrophilic side chains (polar) are on the outside of the molecule.

Properties:
*Soluble in aqeous media
*Have been crystallized and have definite molecular weights
*Can be denatured

A

GLOBULAR

33
Q

Fibrous or Globular:

Found in wool, feathers, hooves, silk, and fingernails.

A

Keratins (Fibrous)

34
Q

Fibrous or Globular:

Found in tendons, bone, and other connective tissues

A

Collagens (Fibrous)

35
Q

Fibrous or Globular:

Found in blood vessels and ligaments

A

Elastins (Fibrous)

36
Q

Fibrous or Globular:

Found in muscle tissue

A

Myosins (Fibrous)

37
Q

Fibrous or Globular:

Found in blood clots

A

Fibrin (Fibrous)

38
Q

Fibrous or Globular:

Regulatory hormone for controlling glucose metabolism

A

Insulin (Gllobular)

39
Q

Fibrous or Globular:

Involved in oxygen storage in muscles.

A

Myoglobin (Globular)

40
Q

Fibrous or Globular:

involved in oxygen transport in blood

A

hemoglobin (globular)

41
Q

Fibrous or Globular:

involved in iron transport in blood

A

transferrin (globular)

42
Q

Fibrous or Globular:

involved in immune system responses

A

immunoglobulins (globular)

43
Q

Identify what is the function of the protein:

Enzymes - biochemical catalyst

A

Catalytic

44
Q

Identify what is the function of the protein:

Immunoglobulins or antibodies (IgG,IgM,IgA,IgE)
- carries oxygen from the lungs to other organs and tissues.
- carries iron from the liver to the bone marrow

A

Transport

45
Q

Identify what is the function of the protein:

Insulin
Glucagon
Human growth hormone
- transmit signals to coordinate biochemical processes between different cells, tissues, and organs

A

Messenger

46
Q

Identify what is the function of the protein:

Actin and myosin
- necessary for all forms of movement

A

Contractile

47
Q

Identify what is the function of the protein:

Collagen
Keratin
- confer stiffness and rigidity to otherwise fluid-like biochemical

A

Structural

48
Q

Identify what is the function of the protein:

Ferritin
Myoglobin
- bind (and store) small molecules for future use

A

Storage

49
Q

Identify what is the function of the protein:

transcription factors (TFs) - protect their binding DNA sequences from nuclease cleavage, resulting in the markedly increased accessibility surrounding their binding sites and over neighboring chromatin
- Act as sites at which messenger molecules, like insulin, can bind and thereby initiate the effect that the messenger “carries.”
- Are often the molecules that bind to enzymes (catalytic proteins), thereby turning them “on” and “off” and thus controlling enzymatic action.

A

Regulatory

50
Q

Identify what is the function of the protein:

Membrane transport proteins (eg. Glucose transporter)
Ligand gated ion channels
- function as gateways to permit the transport of specific substances across the membrane

A

Transmembrane

51
Q

Identify what is the function of the protein:

Casein
Ovalbumin
- particularly important in the early stages of life, from embryo to infant.

A

Nutrient

52
Q

Identify what is the function of the protein:

Hemoglobin has a buffering role in addition to being an oxygen carrier.
- part of the system by which the acid-base balance within body fluids is maintained

A

Buffer

53
Q

Identify what is the function of the protein:

Albumin (serum albumin)
Globulin
- help maintain fluid balance between blood and surrounding tissue

A

Fluid Balance

54
Q

occurs when protein deprivation is relatively greater than the reduction in total calories. It is frequently seen in children after weaning at about one year of age, when their diet consists predominantly of carbohydrates. Typical symptoms include stunted growth, edema, skin lesions, depigmented hair, anorexia, enlarged fatty liver, and decreased plasma albumin concentration. Edema results from the lack of adequate plasma proteins (albumin) to maintain the distribution of water between blood and tissues. Edema may mask muscle loss.

A

Kwashiorkor

55
Q

occurs when calorie deprivation is relatively greater than the reduction in protein. It usually occurs in children younger than 1 year of age when breast milk is supplemented with watery gruels of native cereals that are usually deficient in protein and calories. Typical symptoms include arrested growth, extreme muscle wasting (emaciation), weakness, and anemia

A

Marasmus

56
Q

accumulation of insoluble, long, fibrillar protein assemblies consisting of β-pleated sheets caused by abnormal proteolytic cleavage.

A

Amyloidosis

57
Q

amyloid plaque caused by accumulation of amyloid β (Aβ), a peptide containing 40–42 amino acid residues, which are nonbranching fibrils of Beta pleated sheet. These peptides are neurotoxic, and is the central pathogenic event leading to the cognitive impairment characteristic of the disease. A second biologic factor is the accumulation of neurofibrillary tangles inside neurons. A key component of these tangled fibers is an abnormal form of the tau (τ) protein, which in its healthy version helps in the assembly of the microtubular structure. The defective τ, however, appears to block the actions of its normal counterpart.

A

Alzheimer disease

58
Q

has been strongly implicated as the causative agent of transmissible spongiform encephalopathies (TSEs) (group of rare degenerative brain disorders characterized by tiny holes that give the brain a “spongy” appearance) , including Creutzfeldt-Jakob disease in humans, scrapie in sheep, and bovine spongiform encephalopathy in cattle (popularly called “mad cow disease”)

A

Prion disease

59
Q

An increased concentration of 14-3-3 protein in cerebrospinal fluid

A

Creutzfeldt-Jakob disease

BIO 024: Biochemistry (16 decks)

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