Brainscape's Knowledge GenomeTM


Top Flashcards (Certified)
All Flashcards

BIOCHEM LEC > PRE FI LEC 1: PROTEINS > Flashcards

PRE FI LEC 1: PROTEINS Flashcards

(65 cards)

Start Studying
1
Q

PROTEINS IN THE HUMAN BODY
- fight invaders

A

ANTIBODIES

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

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

A

COMPLEMENT SYSTEM

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

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

A

CYTOKINES

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

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

A

ACTIN & MYOSIN

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

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

A

MYOGLOBIN

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

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

A

FERRITIN

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

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

A

HEMOGLOBIN

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

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

A

FIBRINOGEN

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

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

A

ALBUMIN

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

PROTEINS IN THE HUMAN BODY
- helps break down food

A

DIGESTIVE ENZYMES

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

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

A

CELL MEMBRANE

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

PROTEINS IN THE HUMAN BODY

Cell membrane 3 types of protein?

A

PERIPHERAL PROTEIN
INTEGRAL PROTEIN
LIPID - BOUND PROTEIN

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

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

A

CYTOSKELETON

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

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

A

KERATIN

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

PROTEINS IN THE HUMAN BODY
- structural protein
- provides strength

A

COLLAGEN

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

PROTEINS IN THE HUMAN BODY
- structural protein
- provides flexibility

A

ELASTIN

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

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

A

AMINO ACIDS

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

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

A

15 %

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

Elemental composition of a protien

A

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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

Other elements found in protein are?

A

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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
21
Q

STRUCTURE of an AMINO ACID is composed of:

  • 2 functional groups?
A

AMINE (NH2) & CARBOXYLY GROUP (COOH)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
23
Q

CLASSIFICATION
- aka hydrophobic amino acids

A

NONPOLAR AMINO ACIDS

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
24
Q

CLASSIFICATION
- non-charged AAs

A

POLAR NEUTRAL AMINO ACIDS

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
25
CLASSIFICATION - NEGATIVELY charged at physiological pH –COOH group in the residue is ionized into –COO- at cellular pH
POLAR ACIDIC AMINO ACIDS
26
CLASSIFICATION - POSITIVELY charged at physiological pH –NH2 group in the residue is ionized into –NH3+ at cellular pH
POLAR BASIC AMINO ACIDS
27
NONPOLAR AMINO ACIDS
- GLYCINE - VALINE - ALANINE - LEUCINE - ISOLEUCINE - METHIONINE - PROLINE - PHENYLALANINE - TRYPTOPHAN
28
POLAR NEUTRAL AMINO ACIDS
- SERINE - THREONINE - TYROSINE - CYSTEINE - ASPARAGINE - GLUTAMINE
29
POLAR ACIDIC ACIDS
- ASPARTIC ACID - GLUTAMIC ACID
30
POLAR BASIC AMINO ACIDS
- HISTIDINE - LYSINE - ARGININE
31
widely used for naming
3-LETTER ABBREVIATION
32
commonly used for comparing amino acid sequence of proteins
1-LETTER ABBREVIATION
33
HOW MANY ESSENTIAL AMINO ACIDS ARE THERE?
9
34
HOW MANY NON - ESSENTIAL AMINO ACIDS ARE THERE?
11
35
not naturally occurring, source: dietary intake
ESSENTIAL AMINO ACIDS
36
naturally occurring, produced by the body
NON - ESSENTIAL AMINO ACIDS
37
ESSENTIAL AMINO ACIDS
- PHENYLALANINE - HISTIDINE - ISOLEUCINE - LEUCINE - METHIONINE - THREONINE - TRYTOPHAN - VALINE - LYSINE
38
CONDITIONALLY NON - ESSENTIAL AMINO ACIDS
- ARGININE - ASPARAGINE - GLUTAMINE - GLYCINE - PROLINE - SERINE - TYROSINE
39
NON - ESSENTIAL AMINO ACIDS
- ALANINE - ASPARTATE - CYSTEINE - GLUTAMATE
40
- an ion with + (positive) and – (negative) charges on the same molecule with a net zero charge
ZWITTERIONS
41
- Under physiological conditions, amino acids exists as Zwitterions - Carboxyl groups _________ a proton to get negative charge - Amino groups ___________ a proton to become positive
GIVE-UP; ACCEPT
42
– pH at which the concentration of Zwitterion is maximum - net charge is zero
ISOELECTRIC POINT (pI)
43
- Chemically unique amino acid - the only standard amino acid with a sulfhydryl group ( — SH group)
CYSTEINE
44
Cysteine in the presence of MILD OXIDIZING AGENTS dimerizes to form a ____________ molecule.
CYSTINE
45
are short chains of amino acids linked by peptide bonds.
PEPTIDES
46
- are longer, continuous chains of peptide - have a molecular mass of 10,000 Da or more are called proteins
POLYPEPTIDE
47
The covalent bonds between amino acids in a peptide are called _____________
PEPTIDE BONDS OR AMIDE
48
bond between two amino acids
DIPEPTIDE
49
bond between ~ 10 - 20 amino acids
OLIGOPEPTIDE
50
bond between large number of amino acids
POLYPEPTIDE
51
Every peptide has an ________________ & ______________
N-TERMINAL END; C-TERMINAL END
52
Biochemically important SMALL PEPTIDES
- HORMONES - NEUROTRANSMITTERS - ANTIOXIDANTS
53
- released into the bloodstream as a hormone in response to sexual activity and during labor (HORMONE)
OXYTOCIN
54
- antidiuretic hormone that helps fluid retention in the body to balance water volume and osmolality (HORMONE)
VASOPRESSIN
55
are pentapeptide neurotransmitters produced by the brain and bind receptors within the brain; help reduce pain (NEUROTRANSMITTERS)
ENKEPHALINS
56
- 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
GLUTATHIONE (Glu-Cys-GLy)
57
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
SIMPLE PROTEINS
58
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
CONJUGATED (COMPLEX PROTEINS
59
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
PRIMARY STRUCTURE
60
STRUCTURE OF PROTEIN - 2 most common types : alpha-helix and the beta-pleated sheet
SECONDARY STRUCTURE
61
A single protein chain adopts a shape that resembles a coiled spring
ALPHA - HELIX (a-HELIX)
62
Completely extended amino acid chains
BETA- PLEATED SHEETS
63
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
TERTIARY STRUCTURE
64
4 TYPES OF INTERACTION OBSERVED IN A TERTIARY STRUCTURE
- DISULFIDE BONDING - ELECTROSTATIC INTERACTIONS - H-BONDING - HYDROPHOBIC INTERACTIONS
65
- 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
QUATERNARY STRUCTURE

BIOCHEM LEC (10 decks)

Brainscape helps you reach your goals faster, through stronger study habits.
© 2025 Bold Learning Solutions. Terms and Conditions