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BIOCHEM LEC > PRE FI LEC 1: PROTEINS > Flashcards

PRE FI LEC 1: PROTEINS Flashcards

1
Q

PROTEINS IN THE HUMAN BODY
- fight invaders

A

ANTIBODIES

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2
Q

PROTEINS IN THE HUMAN BODY
- system of 20 PROTEIN molecules that are activated during INFECTIONS

A

COMPLEMENT SYSTEM

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3
Q

PROTEINS IN THE HUMAN BODY
- Signaling proteins
- communicate with other cells

A

CYTOKINES

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4
Q

PROTEINS IN THE HUMAN BODY
- proteins in the muscle
- interaction with each other for muscle movement

A

ACTIN & MYOSIN

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5
Q

PROTEINS IN THE HUMAN BODY
- proteins in the muscle
- release oxygen to muscle

A

MYOGLOBIN

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6
Q

PROTEINS IN THE HUMAN BODY
- proteins in the muscle
- stores and release oxygen

A

FERRITIN

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7
Q

PROTEINS IN THE HUMAN BODY
- proteins in the blood
- transport oxygen

A

HEMOGLOBIN

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8
Q

PROTEINS IN THE HUMAN BODY
- proteins in the blood
- clots blood

A

FIBRINOGEN

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9
Q

PROTEINS IN THE HUMAN BODY
- proteins in blood
- maintain proper amount of liquid in blood

A

ALBUMIN

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10
Q

PROTEINS IN THE HUMAN BODY
- helps break down food

A

DIGESTIVE ENZYMES

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11
Q

PROTEINS IN THE HUMAN BODY
- form channels for substances to move through membrane
- act as enzymes
- act as receptors

A

CELL MEMBRANE

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12
Q

PROTEINS IN THE HUMAN BODY

Cell membrane 3 types of protein?

A

PERIPHERAL PROTEIN
INTEGRAL PROTEIN
LIPID - BOUND PROTEIN

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13
Q

PROTEINS IN THE HUMAN BODY
- structural protein
- network of protein filament and tubules that maintain cell shape

A

CYTOSKELETON

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14
Q

PROTEINS IN THE HUMAN BODY
- structural protein
- found in skin, hair, and nails

A

KERATIN

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15
Q

PROTEINS IN THE HUMAN BODY
- structural protein
- provides strength

A

COLLAGEN

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16
Q

PROTEINS IN THE HUMAN BODY
- structural protein
- provides flexibility

A

ELASTIN

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17
Q

CHARACTERISTICS OF PROTEINS
- A protein is a naturally-occurring, unbranched polymer in
which the monomer units are?

A

AMINO ACIDS

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18
Q

CHARACTERISTICS OF PROTEINS
- Proteins are most abundant molecules in the cells after water
(__% of a cell’s overall mass)

A

15 %

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19
Q

Elemental composition of a protien

A

CARBON, HYDROGEN, OXYGEN, NITROGEN, SULFUR (CHONS)

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20
Q

Other elements found in protein are?

A

IRON (Fe), PHOSPHORUS (P) & some other metals in some specialized protein

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21
Q

STRUCTURE of an AMINO ACID is composed of:

  • 2 functional groups?
A

AMINE (NH2) & CARBOXYLY GROUP (COOH)

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22
Q

STRUCTURE of an AMINO ACID is composed of:

A

○ 2 functional groups: Amine (NH2) and Carboxyl (COOH) Group
○ Side chain or R group
○ Alpha carbon atom

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23
Q

CLASSIFICATION
- aka hydrophobic amino acids

A

NONPOLAR AMINO ACIDS

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24
Q

CLASSIFICATION
- non-charged AAs

A

POLAR NEUTRAL AMINO ACIDS

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25
Q

CLASSIFICATION
- NEGATIVELY charged at physiological pH
–COOH group in the residue is ionized into
–COO- at cellular pH

A

POLAR ACIDIC AMINO ACIDS

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26
Q

CLASSIFICATION
- POSITIVELY charged at physiological pH
–NH2 group in the residue is ionized into
–NH3+ at cellular pH

A

POLAR BASIC AMINO ACIDS

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27
Q

NONPOLAR AMINO ACIDS

A
  • GLYCINE
  • VALINE
  • ALANINE
  • LEUCINE
  • ISOLEUCINE
  • METHIONINE
  • PROLINE
  • PHENYLALANINE
  • TRYPTOPHAN
28
Q

POLAR NEUTRAL AMINO ACIDS

A
  • SERINE
  • THREONINE
  • TYROSINE
  • CYSTEINE
  • ASPARAGINE
  • GLUTAMINE
29
Q

POLAR ACIDIC ACIDS

A
  • ASPARTIC ACID
  • GLUTAMIC ACID
30
Q

POLAR BASIC AMINO ACIDS

A
  • HISTIDINE
  • LYSINE
  • ARGININE
31
Q

widely used for naming

A

3-LETTER ABBREVIATION

32
Q

commonly used for comparing amino acid sequence of proteins

A

1-LETTER ABBREVIATION

33
Q

HOW MANY ESSENTIAL AMINO ACIDS ARE THERE?

A

9

34
Q

HOW MANY NON - ESSENTIAL AMINO ACIDS ARE THERE?

A

11

35
Q

not naturally occurring, source: dietary intake

A

ESSENTIAL AMINO ACIDS

36
Q

naturally occurring, produced by the body

A

NON - ESSENTIAL AMINO ACIDS

37
Q

ESSENTIAL AMINO ACIDS

A
  • PHENYLALANINE
  • HISTIDINE
  • ISOLEUCINE
  • LEUCINE
  • METHIONINE
  • THREONINE
  • TRYTOPHAN
  • VALINE
  • LYSINE
38
Q

CONDITIONALLY NON - ESSENTIAL AMINO ACIDS

A
  • ARGININE
  • ASPARAGINE
  • GLUTAMINE
  • GLYCINE
  • PROLINE
  • SERINE
  • TYROSINE
39
Q

NON - ESSENTIAL AMINO ACIDS

A
  • ALANINE
  • ASPARTATE
  • CYSTEINE
  • GLUTAMATE
40
Q
  • an ion with + (positive) and – (negative) charges on the same molecule with a net zero charge
A

ZWITTERIONS

41
Q
  • Under physiological conditions, amino acids exists as Zwitterions
  • Carboxyl groups _________ a proton to get negative charge
  • Amino groups ___________ a proton to become positive
A

GIVE-UP; ACCEPT

42
Q

– pH at which the concentration of Zwitterion is maximum - net charge is zero

A

ISOELECTRIC POINT (pI)

43
Q
  • Chemically unique amino acid
  • the only standard amino acid with a sulfhydryl group ( — SH group)
A

CYSTEINE

44
Q

Cysteine in the presence of MILD OXIDIZING AGENTS dimerizes to form a ____________ molecule.

A

CYSTINE

45
Q

are short chains of amino acids linked by
peptide bonds.

A

PEPTIDES

46
Q
  • are longer, continuous chains of peptide
  • have a molecular mass of 10,000 Da or more are
    called proteins
A

POLYPEPTIDE

47
Q

The covalent bonds between amino acids in a peptide are called _____________

A

PEPTIDE BONDS OR AMIDE

48
Q

bond between two amino acids

A

DIPEPTIDE

49
Q

bond between ~ 10 - 20 amino acids

A

OLIGOPEPTIDE

50
Q

bond between large number of amino acids

A

POLYPEPTIDE

51
Q

Every peptide has an ________________ & ______________

A

N-TERMINAL END; C-TERMINAL END

52
Q

Biochemically important SMALL PEPTIDES

A
  • HORMONES
  • NEUROTRANSMITTERS
  • ANTIOXIDANTS
53
Q
  • released into the bloodstream as a hormone in
    response to sexual activity and during labor (HORMONE)
A

OXYTOCIN

54
Q
  • antidiuretic hormone that helps fluid retention in
    the body to balance water volume and osmolality (HORMONE)
A

VASOPRESSIN

55
Q

are pentapeptide neurotransmitters produced by
the brain and bind receptors within the brain; help reduce pain (NEUROTRANSMITTERS)

A

ENKEPHALINS

56
Q
  • a tripeptide, present in high levels in most cells, a regulator of oxidation–reduction reactions
  • is an antioxidant and protects cellular
    contents from oxidizing agents such as peroxides
    and superoxides
A

GLUTATHIONE (Glu-Cys-GLy)

57
Q

A protein in which only amino acid residues are present:
More than one protein subunit may be present but all subunits contain only amino acids

A

SIMPLE PROTEINS

58
Q

A protein that has one or more non-amino acid entities (prosthetic groups)
- One or more polypeptide chains may be present

~ Non-amino acid components - may be organic or inorganic - prosthetic groups

Examples: lipoproteins, glycoproteins and metalloproteins

A

CONJUGATED (COMPLEX PROTEINS

59
Q

STRUCTURE OF PROTEIN
- Refers to the order in which amino acids are linked together in a protein; every protein has its own unique amino acid sequence

A

PRIMARY STRUCTURE

60
Q

STRUCTURE OF PROTEIN
- 2 most common types : alpha-helix and the beta-pleated sheet

A

SECONDARY STRUCTURE

61
Q

A single protein chain adopts a shape that resembles a coiled spring

A

ALPHA - HELIX (a-HELIX)

62
Q

Completely extended amino acid chains

A

BETA- PLEATED SHEETS

63
Q

STRUCTURE OF PROTEIN
- The overall three-dimensional shape of a protein
Results from the interactions between amino acid side chains (R groups) that are widely separated from each other

A

TERTIARY STRUCTURE

64
Q

4 TYPES OF INTERACTION OBSERVED IN A TERTIARY STRUCTURE

A
  • DISULFIDE BONDING
  • ELECTROSTATIC INTERACTIONS
  • H-BONDING
  • HYDROPHOBIC INTERACTIONS
65
Q
  • refers to the organization among the
    various polypeptide chains in a multimeric protein:
    ~ Highest level of protein organization
    ~ Present only in proteins that have 2 or more polypeptide chains (subunits)
    ~ are often referred to as oligomeric
    proteins
A

QUATERNARY STRUCTURE

BIOCHEM LEC (10 decks)

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