MOD 2 L1 Flashcards

1
Q

general formula for amino acids

A

amino group - c (with side chain sa baba) - carboxylic acid

NH - C - COOH

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2
Q

most ABUNDANT & FUNCTIONALLY DIVERSE molecules in living systems

A

PROTEINS

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3
Q

it is a LARGE MOLECULE that contains carbon, hydrogen, oxygen, & nitrogen (CHON)

A

PROTEINS

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4
Q

the chiral carbon is also called as

A

α - carbon (alpha carbon)

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5
Q

has 4 different groups attached to it

A

CHIRAL CENTER

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6
Q

what forms a peptide bond in amino acids

A

AMINO GROUP & CARBOXYLIC ACID GROUP

NH & COOH

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7
Q

proteins are

A

POLYPEPTIDE

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8
Q

every function in the living cells are HIGHLY DEPENDENT on

A

PROTEINS

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9
Q

a specialized protein of FLAGELLA is called

A

FLAGELLIN

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10
Q

an example of GLOBULAR PROTEIN

A

HEMOGLOBIN

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11
Q

component of hemoglobin that is RESPONSIBLE FOR THE PIGMENT or the red color of our blood

A

HEME

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12
Q

hemoglobin is a

A

TETRAMERIC

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13
Q

sides / groups of hemoglobin

A

2 - α
2- β

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14
Q

a special nucleus found in hemoglobin is known as

A

PROTOPHORPYRIN

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15
Q

turn genes ON & OFF to guide the differentiation of the cell and its later responsiveness to signals reaching it

A

TRANSCRIPTION FACTORS

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16
Q

the PRIMARY FUNCTION of protein is to provide the needed amino acids for maintaining an

A

ANABOLIC STATE

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17
Q

proteins play a vital role in the ________ system

A

NEURO-ENDOCRINE

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18
Q

one of the by product of protein metabolism

A

UREA

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19
Q

how many amino acids are involved in TRANSLATION

A

20

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20
Q

protein synthesis

A

TRANSLATION

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21
Q

how many amino acids are PRODUCED BY HUMANS?

A

AT LEAST 10

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22
Q

saan manggagaling ung another 10 amino acids that our body cannot produce

A

they must be supplemented in our diet

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23
Q

the other 10 amino acids that our body CANNOT PRODUCE is referred to as

A

ESSENTIAL AMINO ACIDS

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24
Q

what type of amino acids are produced by humans

A

L - α

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25
what type of amino acids are produced by microorganisms
D amino acids
26
predominant amino acid in BACILLUS SUBTILIS
D-METHIONINE
27
Bacitracin & Gramicidin A
ANTIBIOTICS
28
Bleomycin
ANTITUMOR AGENT
29
Microcystin & Nodularin
CYANOBACTERIAL PEPTIDES
30
metabolic product of bacillus subtilis
BACITRACIN
31
has TYROCIDIN
GRAMICIDIN A
32
common side effect of BLEOMYCIN
pulmonary fibrosis
33
toxic microbial peptides
CYANOBACTERIAL PEPTIDES
34
an IMINO ACID
PROLINE
35
all amino acids posses the same functional group except
PROLINE
36
formed by the COOH of an amino acid and the NH₂ of the next amino acid
PEPTIDE BOND
37
peptide bonds has the capability to rotate because of this characteristic
PARTIAL DOUBLE BOND
38
the protation of peptide bonds are termed as
RESONANCE
39
forms a typical peptide group
RESONANCE
40
uncharged, single-bonded form is typically
60%
41
charged, double-bonded form is typically
40%
42
the peptide bond is an __ bond
AMINE BOND
43
these are very STABLE and NEUTRAL
AMIDES
44
amino acids are linked by
PEPTIDE BONDS
45
naming of peptides
drop -ine, palitan ng -yl retained ang name ng terminal amino acid ( yung nasa dulo)
46
useful in classifying amino acids
R GROUP
47
the genetic code specifies how many amino acids
20
48
only what amino acids in human occurs in proteins
L - α amino acids
49
represents the **vast majority** of amino acids found in proteins
L-amino acids
50
found in some **antibiotics** and in the **bacterial cell wall**
D-amino acids
51
# REACTIONS OF AMINO ACIDS responsible for: * acylation * amidation * esterification
AMINE GROUP
52
# REACTIONS OF AMINO ACIDS responsible for: * esterification * formation of amides and acid anhydrides
CARBOXYLIC ACID GROUP
53
the **most important reaction** of amno acids
PEPTIDE BOND FORMATION
54
* tend to **interact with the aqueous environment**, often involved in the formation of H-bonds * predominnatly found on the **exterior surfaces** of proteins or in the reactive centers of enzymes * Ser, Thr, Tyr
HYDROPHILIC AMINO ACIDS
55
* tend to **repel** the aqueous environment * **do not ionize or participate** in the formation of H-bonds * reside predominantly in the **interior** of proteins * Ala, Val, Leu, Ile
HYDROPHOBIC AMINO ACIDS
56
allow enzyme reactions to occur
R GROUPS
57
act as either a **proton donor** or **acceptor** at **physiological pH**, thus play a important role in **enzymatic catalysis**
IMIDAZOLE RING og [H]
58
allow **serine and threonine**, **cysteine** to act as **nucleophiles** during **enzymatic catalysis**
primary alcohol of ser & thr thiol of cys
59
____ of cysteine able to form a **disulfide bonds** with other cysteines
THIOL
60
____ of ser, tyr, and thr participate in the **regulation of activity of enzymes**
OH GROUP
61
amino aids may have positive, negative, or zero net charge
ZWITTERIONS
62
charge of zwitterion
both + & - charge
63
zwitterion is ____ overall
neutral
64
# TESTS * used to **visualize spots or bands of amino acids** separated by **chromatography** or electrophoresis * **deep purple color** is formed with traces of any amino acid * **RUHEMANN'S PURPLE**
REACTION W/ NINHYDRIN
65
# TESTS * **General test for the presence of protein** * turns **purple** when mixed with a solution containing protein * purple color is formed when copper ions in the reagent react with the peptide bonds of the polypeptide chains to form a complex
BIURET TEST
66
requirement of biuret test
should be polypeptide kapag tripeptide, negative ang result
67
# TESTS * used to determine the presence of **aromatic amino acids** * concentrated nitric acid will form a **yellow complex** with **tryptophan** and **tyrosine** side chains in proteins
XANTHOPROTEIC TEST
68
# TESTS test for **tyrosine**
MILLON'S TEST
69
# TESTS test for **tryptophan**
HOPKIN'S
70
# TESTS * **disulfide bridges wil react with Pb²+ ion** from lead acetate in an acidified solution * a **black precipitate (PbS)** indicates the presence of disulfide bonded cysteine in proteins
LEAD ACETATE TEST