Bio1 Molecules/ Fundamentals Flashcards
1
Q
Any substance that takes up space and has mass
A
Matter
2
Q
What matter is composed of?
A
Elements
3
Q
Substance that has specific chemical/physical properties
A
Element
4
Q
Smallest unit of matter/retains all chemical properties of element
A
Atom
5
Q
Combining 2 or more atoms creates a
A
Molecule
6
Q
Atoms carbon tends to bond with in an organic molecule
A
Hydrogen,oxygen,nitrogen
7
Q
Molecules that contain more than one element
A
Compounds
8
Q
Strong attractive forces that hold atoms WITHIN a molecule
A
Intramolecular forces
9
Q
Force that exists BETWEEN molecules
A
Intermolecular forces
10
Q
Is intra or intermolecular forces stronger?
A
Intramolecular forces are stronger
11
Q
Type of force that determines physical properties
A
Intermolecular forces
12
Q
Molecules that have potential of bonding to other identical molecules through chemical reactions
A
Monomers
13
Q
The process which polymers are formed by monomers bonding is called
A
Polymerization
14
Q
3 varieties of carbohydrates
A
Monosaccharides,disaccharides,polysaccharides
15
Q
Monosaccharides have a ratio of precisely
A
1 carbon per water molecule
16
Q
Monosaccharide empirical formula
A
(CH2O)n
17
Q
5 carbon monosaccharides
A
Pentodes
18
Q
6 carbon monosaccharides
A
Hexoses
19
Q
Sugar molecule is ALPHA if hydroxyl Group on first carbon
A
Points down
20
Q
Sugar molecule is BETA if hydroxyl group on first carbon
A
Points up
21
Q
An example of pentose (5carbon sugar)
A
Ribose
22
Q
____ and _____ are examples of hexoses (6carbon sugars)
A
Glucose , Fructose
23
Q
Glucose and fructose are
A
Isomers
24
Q
Type of carbohydrate that forms when 2 monosaccharides bond
A
Disaccharide
25
Monosaccharides monomers bond via which reaction
Dehydration/condensation reactions
26
Functional group and atom that combine in dehydration/condensation reaction
Hydroxyl (OH) and Hydrogen
27
Type of bond in dehydration/condensation reaction
Covalent
28
What is released in a dehydration/condensation reaction?
H2O
29
Opposite of dehydration/condensation reaction
Hydrolysis; adds H2O to covalent bond splits monomers apart
30
Bond that forms when carbohydrate attaches to another molecule
Glycosidic
31
Carbohydrates linked to lipids are called
Glycolipids
32
Carbohydrates linked to proteins
Glycoproteins
33
1glucose + 1 fructose =
Sucrose
34
1 galactose + 1 glucose=
Lactose
35
1 glucose + 1 glucose=
Maltose
36
Polysaccharides are long polymers of
Monosaccharides
37
2 polysaccharide purposes
Storage, structure
38
Crucial storage polysaccharide in plants
Starch
39
Starch contains many glucose monomers in____ and ____ forms
Linear, branched
40
Linear plant starch
Amylose
41
Type of glycosidic bonds in amylose
Alpha-1,4- glycosidic bonds
42
Branched form of plant starch
Amylopectin
43
Type of bonds in amylopectin
- Alpha1,4 glycosidic (linear)
| - Alpha1,6 glycosidic (branched)
44
Storage polysaccharide found in humans
Glycogen
45
Glycogen contains many
Glucose monomers
46
Which is more branched amylopectin or glycogen?
Glycogen more branched
47
Types of bonds glycogen
- alpha 1,4 glycosidic
| - MANY alpha 1,6 glycosidic
48
Glycogen primarily stored in what type of human cells?
Liver cells(mostly) ; also muscle cells
49
Name 2 alpha glucose polysaccharides
Starch(amylose or amylopectin) and glycogen
50
Structural polysaccharide found in plant cell walls, wood and paper
Cellulose
51
Cellulose is a ___
Glucose polymer
52
Type of bonds in cellulose
Beta 1,4 glycosidic bonds
53
What beta 1,4 glycosidic bonds in cellulose do?
Allow cellulose to form linear strands that pack together parallel
54
Intermolecular force that holds adjacent cellulose strands together in parallel
Hydrogen bonds
55
Due to its structure cellulose has
High rigidity
56
Can humans digest cellulose?
No; it passes through digestive tract as fiber
57
Chitin is a __
Structural polysaccharide
58
Chitin is found in ____ and ____
Fungi cell walls, insect exoskeleton
59
Chitin is a structural polysaccharide of ____
N-acetylglucosamine monomers
60
Types of bonds in chitin
Beta 1,4 glycosidic bonds
61
Two beta glucose polysaccharides
Chitin and cellulose
62
Proteins contain polymers called
Polypeptides
63
Polypeptides contain monomeric subunits called
Amino acids
64
4 things central carbon in amino acid bonded to
- amino group(NH2)
- Hydrogen atom
- carboxyl group(COOH)
- R group
65
Total number of amino acids
20
66
Amino acids are linked via covalent bond called
Peptide bond
67
Amino acids form peptide bonds via
Dehydration/condensation reactions
68
Reactions that separate amino acids of polypeptide
Hydrolysis
69
Enzyme that catalyzes peptide bond formation
Peptidyl transferase
70
Peptidyl transferases are ___
Aminoacyl transferases
71
Polypeptides have a ___ terminus and a ____ terminus
Amino(N-) ; carboxyl(C-)
72
Primary structure of a protein
It’s amino acid sequence
73
All proteins have
Primary structure
74
Secondary structure of protein
Folds due to intermolecular forces between atoms of polypeptide backbone
75
All the amino acid structural features EXCLUDING R group
Polypeptide backbone
76
Secondary structure does not include
Interactions between R group atoms
77
Which level protein structure includes alpha helices and beta pleated sheets?
Secondary
78
Most common intermolecular force for secondary structure? And where do they occur?
Hydrogen bonding; occurs between carboxyl(COOH)and amino groups(NH2
79
The common interactions between R groups in tertiary structure
- Ionic bonding
- Hydrogen bonding
- Dipole-dipole interactions
- Van see Waal( London dispersion forces)
- Hydrophobic interactions
- Disulfide bonding
80
Tertiary structures usually involve
Non-covalent interactions
81
Bond in tertiary structures that involve covalent interactions
Disulfide bond
82
Which amino acids allow disulfide bond formation?
Cysteine
83
Structure that refers to large proteins that have multiple subunits(multiple polypeptide chains)
Quaternary
84
Multiple polypeptide chains in a quaternary structure, entire structure is
Protein
85
Causes proteins to lose secondary,tertiary,quaternary structures
Protein denaturation
86
Denatured proteins retain
Primary structure
87
Loss of shape leads to
Loss of protein function
88
Causes of protein denaturation
- excess temp
- chemicals
- pH changes
- Radiation
89
3 structural classifications of proteins
- fibrous
- globular
- intermediate
90
Intermediate and globular structural proteins are
Soluble
91
Fibrous structural proteins are
Insoluble
92
Protein that forms structural component of cells
Fibrous structural protein
93
Example of fibrous protein
Collagen
94
Proteins that are folded tightly and perform many functions
Globular
95
Example of globular structural protein
Albumin
96
Fiber shaped proteins that perform many functions
Intermediate
97
Example of intermediate structural protein
Fibrinogen
98
The 2 compositional protein classifications are
Simple, conjugated
99
Simple protein compositions contain only
Amino acids(ex: albumin)
100
Conjugated protein compositions contain
Amino acids+ non protein components
101
Examples of conjugated proteins
Glycoproteins (mucin)
Metalloproteins(hemoglobin)
Lipoproteins(LDL/HDL)
102
Molecules that increase reaction rates
Catalyst
103
What part of reaction do catalysts not affect?
Spontaneity
104
Catalysts are not
Used up in reaction; they manipulate meaning reaction does not change them
105
Catalysts lower this to speed up reaction
Activation energy/transition state energy
106
Catalysts cannot change
Energy absorbing(endothermic) reactions to ——-> energy releasing(exothermic) reactions and vice versa
107
Catalysts do not affect energy of
Reactants or products
108
Biological, globular protein catalysts are
Enzymes
109
Substrates bind to enzymes at the
Active site
110
Active sites have unique properties and
Substrate specificity
111
Measures how efficient enzyme is converting substrate to product
Scecificity constant
112
Enzymes bind at active site via
Induced fit model
113
Example of RNA enzyme
Ribozyme
114
Non protein molecules that assist enzymes
Cofactors
115
Cofactors usually help enzymes by donating/accepting a component such as
Electrons
116
Organic cofactors (ex vitamins)
Coenzymes
117
Inorganic cofactors are
Metal ions ( iron, magnesium)
118
Enzymes that are bound to their cofactor
Holoenzymes
119
Enzymes not bound to cofactor
Apoenzyme
120
Cofactors that tightly/covalently bind to their enzyme in holoenzyne
Prosthetic groups
121
Proteins have highest enzymatic activity when ____ and____ are in optimal ranges
pH and temp
122
Enzyme regulation where inhibitors compete with substrate for active sites
Competitive inhibition
123
Can outcompete competitive inhibitor by
Adding more substrate
124
What is enzyme saturation
When all the active sites are occupied
125
Inhibitor binds to allosteric site of enzyme
Non competitive inhibition
126
Different location then active site of enzyme catalysis
Allosteric site
127
Non competitive inhibitor binds to allosteric site modifies the
Active Site ;so substrate has reduced/inability to bind
