Condensed Lecture from Biological Molecules Flashcards

1
Q

recognized as the most diverse among biomolecules | believed to be the central compound necessary for life | called as Life’s Building Blocks

A

proteins

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

how many percent of organism’s weight is composed and can be attributed to protein?

A

75%

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

amino acid that cannot be produced by our body

A

essential amino acid

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

name the essential amino acids

A

HISTIDINE
ISOLEUCINE
LEUCINE
METHIONINE
PHENYLALANINE
THREONINE
TRYPTOPHAN
VALINE
LYSINE

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

amino acid that can be produced by out body

A

nonessential amino acid

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

name the nonessential amino acids

A

ALANINE
ASPARTATE
CYSTEINE
GLUTAMATE

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

amino acids that are not vital but may become urgent during health crisis and stress

A

conditional amino acid

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

name the conditional amino acids

A

ARGININE
ASPARGININE
GLUTAMINE
GLYCINE
PROLINE
SERINE
TYROSINE

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

explain the process on how proteins are formed from amino acids

A

body - brain - DNA instruction
DNA - mRNA
instruction from mRNA to build proteins

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

the simplest structure of all protein | composed of a linear sequence of amino acid

A

primary structure

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

3d shape created by several hydrogen bonds

A

secondary structure

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

the first 2 pattern of secondary structure were created by

A

Linus Pauling and Robert Corey in 1951

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

3d shape either fibrous or globular

A

tertiary structure

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

proteins with one more polypeptide

A

quaternary structure

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

contain coded instructions for cellular activities such as growth and reproduction death and production and acceptance of certain substances | specifies the right sequence of amino acids to create a particular protein

A

DNA

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

encoding and decoding and regulating the expression of genes, depending on the type of DNA present

A

RNA

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

an RNA that serves as a temporary copy of a gene in the DNA

A

mRNA

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

translates the sequence of nucleic acids in a gene to create the correct sequence of amino acids in a polypeptide

A

tRNA

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

forms peptide bonds between amino acids in a polypeptide

A

rRNA

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

sugar that does not contain oxygen

A

deoxyribose

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

two carbon nitrogen ring bases

A

purines: adenine and guanine

22
Q

one carbon nitrogen base

A

thymine and cytosine

23
Q

special nucleotide that is incorporated in the nucleic acid | battery that produces the highest source of energy in cells

24
Q

a series of chemical reactions in the body that converts food into energy

A

metabolism

25
refer to the sequence of enzyme catalyzed reactions that lead to the conversion of a substance into a final product
metabolic pathways
26
process involving the breakdown of molecules to release energy
catabolism
27
examples of catabolism
polysaccharide to monosaccharide
28
process that requires and consumes energy to allow the building process to start
anabolism
29
examples of anabolism
mineralization of bones from inorganic substances
30
organic catalysts that regulates and controls the metabolic pathways
enzymes
31
components of an enzyme
apoenzyme cofactor
32
protein, proenzyme when inactive and is a polypeptide or protein part of the enzyme
apoenzyme
33
non protein, assists apoenzymes in their biological activities
cofactor
34
not permanently bound and supplies positive charges to the enzymes
metal ion activators
35
organic molecules that usually come from the vitamins that we take everyday and temporarily binds to apoenzymes
coenzymes
36
binds to apoenzymes permanently and can either be metal ions and organic molecules
prosthetic cofactors
37
apoenzyme + cofactor = ?
holoenzyme
38
molecules that an enzyme works on
substrate
39
pocket or groove where the chemical reaction takes place
active site
40
substrate temporarily binds to active site held in by hydrogen and ionic bonds
enzyme-substrate complex
41
Part of coenzyme cocarboxylase: has several functions, including metabolism of pyruvate
B1 Thiamine
42
Coenzyme in Flavoproteins; helps transfer electrons
B2 Riboflavin
43
Coenzyme in Amino Acid Metabolism
B6 Pyridoxine
44
Helps transfer methyl group, active in amino acid metabolism
B12 Cyanocobalamin
45
Part of Nicotinic Acid Dinucleotide (NAD) molecule; helps transfer electrons
Niacin Nicotinic Acid
46
Part of coenzyme A; metabolism of pyruvate and lipids
Panthothenic Acid
47
Helps in carbon dioxide fixation reaction and fatty acid synthesis
Biotin
48
Coenzyme involved in synthesis of purines and pyrimidines
Folic Acid
49
Coenzyme involved in cellular and molecular synthesis
Vitamin E
50
Coenzyme used in electron transport (naphthoquinones & quinones)
Vitamin K