Microbiology & Biochemistry Flashcards

1
Q

TYPICAL BIOLOGICAL PROCESS

A

stock culture
shake flask
seed fermenter

raw material
medium formulation
sterilization

recovery
puriffication -> product
effluent treatment

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2
Q

Diagram Protist Kingdom

A

Prokaryotes
- blue green algae
- bacteria
a. archaeobacteria
b. eubacteria

Eukaryotes
- Algae
- Protozoa
- Fungi
a. molds
b. yeast

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3
Q

a region bounded by a
complex membranous structure called
nuclear envelop.

A

nucleus

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4
Q

nucleus, a region bounded by a
complex membranous structure called

A

nuclear envelop.

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5
Q

a poorly
demarcated region of the cell that lacks a
boundary membrane to separate it from
surrounding cytoplasm.

A

nucleoid

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6
Q

prokaryotic cell length

A

1-5 micrometers

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7
Q

eucaryotic cell length

A

10-30 micrometers

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8
Q

PROKARYOTIC CELLS parts

A

– Cell wall
– Plasma membrane
– Ribosomes
– Flagella
– Pili

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9
Q
  • They do not have a nucleus
  • They have no membrane-bound
    organelles
A

PROKARYOTIC CELLS

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10
Q

Contain several orders of magnitude of
more genetic information

A

EUCARYOTIC CELLS

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11
Q

EUCARYOTIC CELLS length of dna

A

4.6mm (yeast)

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12
Q

Chromosome consists of fibers
containing both

A

DNA and protein

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13
Q

Contain relatively small amount of DNA

A

PROKARYOTIC CELLS

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14
Q

PROKARYOTIC CELLS length of DNA

A

0.25mm to
3mm

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15
Q

in PROKARYOTIC CELLS, cytoplasm is essentially ____________

A

devoid of
membranous structure

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16
Q

In EUCARYOTIC CELLS, cytoplasm is filled with a

A

great diversity of
structures

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17
Q

No condensation of chromosomes and no
spindle apparatus

A

PROKARYOTIC CELLS

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18
Q

The DNA in PROKARYOTIC CELLS is ________
and the two copies are simply separated
by the growth of an intervening cell
membrane

A

duplicated

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19
Q

EUCARYOTIC CELLS - divide by a complex process of ______in
which duplicated chromosomes _______________
into compact structures that are separated
by an elaborate microtubule-containing
apparatus

A

mitosis , condense

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20
Q

Possess complex loco motor mechanism

A

EUCARYOTIC CELLS

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21
Q

Simple locomotion mechanism

A

PROKARYOTIC CELLS

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22
Q

Plant Cell example of

A

EUKARYOTIC CELLS

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23
Q

parts of EUKARYOTIC CELLS

A

– Nucleus
– Plasma membrane
– Organelles
a. Endoplasmic recticulum
+ Rough
+ Smooth
b. Golgi Complex
c. Mitochondrion
d. Lysosome
e. Chloroplast

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24
Q

3 parts usually cannot be seen in the most plant cells

A
  1. Flagellum
  2. Centriole
  3. Lysosome
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25
3 parts usually cannot be seen in the animal cells
cell wall central vacuole chloroplast
26
**double membrane-bound organelles** which are the sites of photosynthesis.
Chloroplast
27
The inner membrane of a Chloroplast forms a **series of stacked plates** called
granum
28
These contain the **pigments** that **absorb light energy**
granum
29
The Seat of Power
Mitochondria
30
These are also bound by a double membrane.
Mitochondria
31
The inner membrane of Mitochondria is the site of the
electron transport system
32
like the ER, is a series of folded membranes.
Golgi Complex
33
It functions in processing enzymes and other products of the ER to a finished product.
Golgi Complex
34
Golgi Complex is the source of the production of .
lysosomes
35
Site for the synthesis of lipids, phospholipids, and steroids
SMOOTH ENDOPLASMIC RECTICULUM
36
Enzymes in the smooth ER regulate the release of
sugar into the bloodstream
37
Functions to store calcium ions
SMOOTH ENDOPLASMIC RECTICULUM
38
required for muscle contraction
Ca+ ions
39
Houses the chromatin
NUCLEUS
40
mass of DNA and protein
chromatin
41
In the nucleus, during cell division the chromatin coils up into recognizable
chromosomes
42
double membrane perforated with pores that allow transport of materials back and forth to the cyotplasm
Nuclear envelope
43
Nuclear envelope is the double membrane perforated with pores that allow transport of materials back and forth to the _______
cytoplasm
44
Site of DNA replication and RNA synthesis (transcription).
NUCLEUS
45
It is the site of the control of gene expression
NUCLEUS
46
Rough because imbedded in the membrane are
ribosomes
47
Site of the synthesis of secretory proteins.
ROUGH ENDOPLASMIC RECTICULUM
48
Site for the synthesis of membrane.
ROUGH ENDOPLASMIC RECTICULUM
49
Enzymes synthesize ___________________ that forms all the membranes of the cell.
phospholipid
50
Site of respiration and convert the chemical energy of sugars and other organic compounds into the highenergy phosphate bonds of an ATP molecule
Mitochondria
51
Refers to the number of cells, not the size of the cell
Microbial Growth
52
Requirements for growth
– Physical * Temperature * Osmotic Pressure * pH – Chemical * Macro nutrients * Micro nutrients
53
Most bacteria grow between pH ______
6.5 - pH 7.5
54
3 types of Temperature Requirements
psychrophiles (cold loving: 0 C - 20 C) mesophiles (moderate temp. loving: 20 C - 40 C) Thermophiles (heat loving: 40 C - 100 C)
54
Very few can grow at below pH
4.0
55
many foods, such as sauerkraut, pickles, and cheeses are preserved from spoilage by acids produced during ____________________
fermentation
56
3 types of Tonicity based on osmotic pressure
hypotonic, isotonic, hypertonic
57
needed in concentrations larger than 10-4 M (chemical reqs)
* Macro
58
needed in concentrations of less than 10-4 M (chemical reqs)
Micro Elements
59
Carbon, nitrogen, hydrogen, sulfur, phosphorus, Mg2+ , and K+ example of?
Macro
60
Mo2+, Zn2+, Cu2+, Mn2+, Ca2+, Na+ , vitamins, growth hormones, and metabolic precursors example of?
micro
61
– major sources cellular carbon and energy
– Carbon
62
use organic compounds such as carbohydrates, lipids, and hydrocarbons as carbon and energy source
Heterotrophs
63
use carbon dioxide as a carbon source.
Autotrophs
64
use carbon dioxide as carbon source and obtain energy from the oxidation of inorganic compounds
Chemoautotrophs
65
use carbon dioxide as carbon source and light as energy source
Photoautotrophs
66
constitutes about **10 – 14%** of cell dry weight
Nitrogen
67
following are sources of? ammonia and ammonium salts (NH4Cl, (NH4)2SO4, NH4NO3,**proteins, peptides, and amino acids**
Nitrogen
68
Incorporated into cell mass in the form of **proteins and nucleic acid**
Nitrogen
69
Present in all organic cell components and cellular water and constitutes **about 20% of the dry weight** of the cell
Oxygen
70
___________ is required as a terminal electron acceptor in the aerobic metabolism of carbon compounds
Molecular oxygen
71
Classification of bacteria basedon their oxygen requirements
1. Obligate Aerobes 2. Obligate Anaerobes 3. Facultative Aerobes/ Anaerobes 4. Microaerophilic
72
Superoxide is toxic to
cells (steals electrons)
73
___________ may produce superoxides (O2-)
All organisms
74
Superoxide must be
neutralized
75
Constitutes about **8% of cell dry** weight and is derived primarily from carbon compounds such as carbohydrates
Hydrogen
76
Hydrogen constitutes about 8% of cell dry weight and is derived primarily from
carbon compounds such as carbohydrates
77
Some bacteria can utilize _________ as an energy source
hydrogen
78
Most common sources are KH2PO4 and K2HPO4
Phosphorus
79
Constitutes about **3% of cell dry weight** and is present in *nucleic acids and in the cell wall* of some grampositive bacteria.
Phosphorus
80
Phosphorus Constitutes about 3% of cell dry weight and is present in
1. nucleic acids and in the 2. cell wall of some gram-positive bacteria.
81
– Constitutes **nearly 1% of the cell dry weight** and is present in proteins and some coenzymes
Sulfur
82
Sulfur constitutes nearly 1% of the cell dry weight and is present in
proteins and some coenzymes
83
most common source of sulfur
(NH4)2SO4
84
A cofactor for some enzymes and is required in carbohydrate metabolism
Potassium
85
Potassium is a cofactor for some enzymes and is required in
carbohydrate metabolism
86
A cofactor of some enzymes and is present in **cell walls and membranes**
Magnesium
87
source of Magnesium
MgSO4 , MgCl2
88
Magnesium is a cofactor of some enzymes and is present in
cell walls membranes
89
the exact chemical composition is known
Chemically Defined Culture Media
90
used to grow fastidious organisms
Chemically Defined Culture Media
91
Inhibits the growth of some bacteria while selecting for the growth of others
Selective Media Culture Media
92
Brilliant Green Agar
Selective Media Culture Media
93
inhibits and select in Brilliant Green Agar and EMB (Eosin Methylene Blue)
– dyes inhibit the growth of Gram (+) bacteria – selects for Gram (-) bacteria
94
Most G.I. Tract infections are caused by
Gram (-) bacteria
95
two sample of selective media culture media
Brilliant Green Agar EMB (Eosin Methylene Blue)
96
Differentiates between different organisms growing on the same plate
Differential Media Culture Media
97
used to differentiate different types of Streptococci (Differential Media)
Blood Agar Plates (TSA with 5% sheep blood)
98
used to identify Salmonella
– MacConkey’s Agar
99
* used to identify Staphylococcus aureus
Mannitol Salt Agar
100
* High salt conc. (7.5%) inhibits most bacteria
Mannitol Salt Agar
101
* pH Indicator (Turns Yellow when acid)
Mannitol Salt Agar
102
Bile salts and crystal violet (inhibits Gram (+) bacteria) also pH indicator
– MacConkey’s Agar
103
non-pathogenic bacteria can _______ lactose, Salmonella can not
ferment
104
– Reducing Media – Anaerobic Container – Agar Stab – Agar Shake
* Anaerobic Bacteria
105
grow best under reduced O2 levels and increased CO2 levels
* Microaerophilic Bacteria
106
* Microaerophilic Bacteria O2 and CO2 %
21 % O2 0.3 to .03 % CO2
107
Generation time (doubling time) – time required for a cell to divide (About 1-3 hours)
Binary Fission
108
Binary Fission for ecoli
20 minutes
109
Binary Fission for Mycobacterium tuberculosis
24h
110
– Lack of food, water or nutrients – space – accumulation of metabolic wastes – lack of oxygen – changes in pH – temperature
Limiting Factors in the Environment
111
Yeast cell > developing bud > new bud > chain of bud
Budding
112
Bacteria are first introduced into an environment or media.
Lag Phase
113
Number of cells changes very little
Lag Phase
114
Bacteria are “checking out” their surroundings.
Lag Phase
115
1 hour to several days
Lag Phase
116
Rapid cell growth (exponential growth)
Log Phase
117
Population doubles every generation
Log Phase
118
In the log phase, they are Microbes that are sensitive to adverse condition
– antibiotics – anti-microbial agents
119
Death rate = rate of reproduction
Stationary Phase
120
* cells begin to encounter environmental stress – lack of nutrients – lack of water – not enough space – metabolic wastes – oxygen – pH
Stationary Phase
121
Death rate > reproduction
death phase
122
caused of death phase
limiting factors in the environment
123
* Using **counting chamber**
Direct Count of Cells
124
* using **fluorescent dyes**
Direct Count of Cells
125
Viable Count – colony forming units (CFU)
Indirect Count of Cells
126
Most Probable Number (MPN)
Indirect Count of Cells
127
dry weight/ml
Direct Measurement of Microbial Cells
128
Measurement of turbidity (optical density)
Indirect Measurement of Microbial Biomass
129
Enumeration of Bacteria
1. Direct Count of Cells 2. Indirect Count of Cells 3. Direct Measurement of Microbial Cells 4. Indirect Measurement of Microbial Biomass
130
Stars (with assistance from the Big bang) have formed ____ stable chemical elements in the universe
83
131
95% of the mass of all terrestrial organisms composed of just 4 of them
– Hydrogen (61% in humans) – Oxygen (26% in humans) – Carbon (10.5% in humans) – Nitrogen (2.4% in humans)
132
– about 90% by mass of all life is
water
133
Liquid water is abundant on Earth thanks to our distance from
sun (temperature)
134
It is a good temperature buffer
water
135
It can absorb much heat before its temperature changes
water
136
– When it does vaporize, it takes much heat with it, cooling down its original location
water
137
electronic structure allows it to form chains
carbon
138
Need bonds to be stable but breakable
carbon
139
Chains of atoms and chains of molecules
carbon
140
At temperatures at which water is liquid, _______ bonds are stable but breakable
carbon
141
prominent in biological compounds due to its **reactivity with carbon and its propensity to form chains** in organic compounds
nitrogen
142
Made of C, H & O
Carbohydrates
143
(CH2O)
Carbohydrates
144
simple sugars with multiple OH groups
Monosaccharides
145
Monosaccharides based on number of carbons (3, 4, 5, 6), a monosaccharide is a ________
triose, tetrose, pentose or hexose.
146
Based on number of _______ (3, 4, 5, 6), a monosaccharide is a triose, tetrose, pentose or hexose.
carbons
147
2 monosaccharides covalently linked
Disaccharides
148
a few monosaccharides covalently linked
Oligosaccharides
149
polymers consisting of chains of monosaccharide or disaccharide units
Polysaccharides
150
in many plant and animal tissues
glucose
151
in many fruits
fructose
152
component of milk
galactose
153
four major classes of biological macromolecules
Proteins, carbohydrates, nucleic acids, and lipids
154
monomer of DNA
nucleotides
155
monomer of carbohydrates
monosaccharides
156
monomer of proteins
amino acids
157
monomer of lipids
glycerol/fatty acids
158
have an aldehyde group at one end.
Aldoses
159
example of Aldoses
glucose
160
have a keto group, usually at C2
Ketoses
161
example of Ketoses
fructose
162
a biopolymer system comprising predominantly of two polysaccharides
Starch
163
two polysaccharides of Starch
amylose and amylopectin
164
For sugars with more than one chiral center, __________ refers to the asymmetric C farthest from the aldehyde or keto group
D or L
165
mirror images of one another
D or L
166
Most naturally occurring sugars are
D isomers
167
a disaccharide with an a(1-4) glycosidic link between C1 - C4 OH of 2 glucoses
Maltose
168
* It is the a anomer
Maltose
169
a product of cellulose breakdown
Cellobiose
170
otherwise equivalent b anomer
Cellobiose
171
O on C1 points up
b
172
C1 O points down
a
173
b(1-4) glycosidic linkage is represented as a
zig-zag
174
one glucose is actually ___________ relative to the other
flipped over
175
Polymers composed of sugars
Polysaccharides
176
* Similar to synthetic polymers
Polysaccharides
177
Uses include energy storage, component of extra cellular matrix (hyaluronan)
Polysaccharides
178
component of extra cellular matrix
hyaluronan
179
animals use to store excess sugar
glycogen
180
plants use to store excess sugar
plant starch
181
fibers that give plants their rigidity & strength
cellulose
182
the basic building block of starch
Glucose
183
The smaller of the two polysaccharides which make up starch
Amylose
184
s a linear molecule comprising of (1-4) linked alpha-D-glucopyranosyl units
Amylose
185
The larger of the two components
Amylopectin
186
highly branched with a much greater molecular weight
Amylopectin
187
This structure contains **alpha-D-glucopyranosyl** units linked mainly by (1-4) linkages (as amylose) but with a **greater proportion of (1-6) linkages**, which gives a large **highly branched structure.**
Amylopectin
188
has been found to form the basis of the structure of starch granules
Amylopectin
189
the short branched (1-4) chains are able to form helical structures which crystallize
Amylopectin
190
major structural component of woody plants and natural fibers
cellulose
191
a ß-Dglucose polymer found in vegetable matter
cellulose
192
in cellulose give the glucose rings a different relative orientation than is found in starch
ß-glycoside linkages
193
human being are not able to digest them
ß-glycoside linkages in cellulose
194
Lipids and Phospholipids
195
Long hydrocarbon chains with active group on one end
Lipids and Phospholipids
196
Store more energy than CHOs because the chains are longer
Lipids and Phospholipids
197
fatty acid derivatives found in cell membranes
Lipids and Phospholipids
198
Structure formation is analogous to surfactant, block copolymer
Lipids and Phospholipids
199
Structure formation of surfactant and Lipids and Phospholipids
block copolymer
200
classes of lipid
- compound - derived lipids - glycolipids - phospholipids - sterols - simple
201
FA’s esterified with glycerol
simple
202
same as simple, but with other compounds also attached
compound
203
fats containing **phosphoric acid** and **nitrogen (lecithin)**
phospholipids
204
FA’s compounded with CHO, but no N
glycolipids
205
substances from the above derived by hydrolysis
derived lipids
206
**large molecular wt. alcohols** found in nature and combined w/FA’s (e.g., cholesterol)
sterols
207
provide means whereby **fat-soluble nutrients** (e.g., sterols, vitamins) can be **absorbed** by the body
Lipids
208
**structural element** of cell, **subcellular** components
Lipids
209
components of **hormones** and **precursors for prostaglandin** synthesis
Lipids
209
concentrated sources of energy (9.45 kcal/g)
Lipids
210
no C-C double bond
Saturated
211
C-C double bond
Unsaturated
212
* Naming convention for fatty acids
Chain length:number of double bonds
213
16:0
palmitic
214
18:2
linoleic
215
 consist of one carboxyl group (-COOH) attached to a non-polar hydrocarbon tail.
Fatty acids
216
most distant carbon is designated
w (omega)
217
e carbon next to the –COOH group is designated
alpha then beta ....
218
* Needed by the body but can not be synthesized
Fatty Acids
219
External source required
Fatty Acids
220
Contains C, H, O and N
Proteins
221
Polymers composed of amino acid monomers
Proteins
222
The amino acid polymers are also called
polypeptides
223
characterized by a specific primary structure – order of mers in the backbone
Proteins
224
In protein, control of ___________ leads to control of 3D structure
primary structure
225
builds information into the molecule that translates into function
control of protein structure
226
can be synthesized in the body
Non-essential
227
# * must be consumed in the diet
Essential
228
cannot be synthesized due to illness or lack of necessary precursors
* Conditionally essential
229
Premature infants lack sufficient enzymes needed to create
arginine
230
bonds link amino acids
Peptide
231
Formed through condensation
Amino Acids
232
Broken through hydrolysis
Amino Acids
233
Amino Acids formed when the ________ of one amino acid joins with the _________ of a second amino acid
acid group (COOH) amine group (NH2)
234
Amino acids share many features, differing only at the
R substituent
235
Amino acids are
left-handed
236
Sugars are
right-handed
237
Once a preponderance of one chirality occurred it was
replicated
238
They couldn’t eat our food
ET organism (right handed) - made up of amino acids
239
DNA encoding combinations
AT, TA, GC or CG
240
DNA encoding Three rungs of four letters gives
64 possible arrangements * This is too many! But, redundancy OK
241
DNA encoding Two rungs of four letters makes
16 combinations. * Not enough to specify each of 20 proteins!
242
Each gene (three rungs) matches up chemically to one of the __________ used by life
20 amino acids
243
Each gene ‘spells’ the name of an
amino acid!
244
The amino acids line up along the __________ according to the map spelled out by the sequences of sets of three rungs
double helix
245
The _______ are like the map on the floor.
rungs of the double helix
246
They spell out which amino acid should line up where
rungs of the double helix
247
– Resembles a twisted ladder
double helix
248
“rails” of the DNA ladder are made of the
sugar and phosphate
249
The “rungs” of the ladder are composed of __________ of the nitrogenous bases
one of four pairs AT, TA, GC or CG
250
One of four “nitrogenous bases”
* Adenine (A) * Guanine (G) * Cytosine (C) * Thymine (T)
251
* Adenine (A) * Guanine (G) * Cytosine (C) * Thymine (T) collectively called
“nucleotides”
252
complex molecule which is built of three basic types of monomers sugar, phosphate, one of four nitrogenous bases
DNA
253
DNA built with
sugar, phosphate, one of four nitrogenous bases
254
Contains C, H, O, N plus P
Nucleic Acids
255
Formed by bonding of individual units called nucleotides
Nucleic Acids
256
Store and transmit hereditary information
Nucleic Acids
257
Examples: – DNA (deoxyribonucleic acid) – RNA (ribonucleic acid)
Nucleic Acids
258
Alteration of the protein’s shape and thus functions through the use of – Bases – Acids – Mechanical agitation – Salts – Heat
Denaturing
259
Primary structure is unchanged by
Denaturing
260
* non-linear * 3 dimensional hemoglobin
Quaternary Structure
261
occurs in the cytosol
Protein Interaction
262
in close proximity to other folded and packed proteins
Protein Interaction
263
involves interaction among tertiary structure elements of separate polymer chains
Protein Interaction
264
* non-linear * 3 dimensional myoglobin
Tertiary Structure
265
occurs in the cytosol (~60% bulk water, ~40% water of hydration)
Protein Packing
266
involves interaction between secondary structure elements and solvent
Protein Packing
267
* yields tertiary structure
Protein Packing
268
* non-linear * 3 dimensional * localized to regions of an amino acid chain
Secondary Structure
269
formed and stabilized by hydrogen bonding, electrostatic and van der Waals interactions
Secondary Structure
270
occurs in the cytosol * involves localized spatial interaction among primary structure elements, i.e. the amino acids
Protein Folding
271
* yields secondary structure
Protein Folding
272
* linear * ordered * 1 dimensional * sequence of amino acid polymer
Primary Structure
273
by convention, written from amino end to carboxyl end
Primary Structure
274
a perfectly linear amino acid polymer is neither functional nor energetically favorable  folding
Primary Structure
275
energetically favorable 
folding
276
occurs at the ribosome
Protein Assembly
277
involves polymerization of amino acids attached to tRNA
Protein Assembly
278
* yields primary structure
Protein Assembly
279
Primary
Assembly
280
Secondary
Folding
281
Tertiary
Packing
282
Quaternary
Interaction
283
alpha helix –
regular helix
284
beta sheet
extended zig-zag
285
beta turn
– puts fold into beta sheet
286
refers to secondary structure stabilized by H bonds – defines protein folding
Tertiary structure
287
refers to local chain conformations – four types are known – alpha helix – regular helix – beta sheet – extended zig-zag – beta turn – puts fold into beta sheet – Globular or random coil
Secondary structure
288
Four Level of Structure protein
– Primary – Secondary – Tertiary – Quaternary
289
Any alteration in the structure or sequencing changes the
shape and function of the protein
290
Made up of chains of amino acids
Proteins
291
classified by number of amino acids in a chain
Proteins
292
fewer than 50 amino acids
Peptides
293
2 amino acids
Dipeptides
294
3 amino acids
Tripeptides
295
more than 10 amino acids
Polypeptides
296
100 to 10,000 amino acids linked together
Proteins
297
synthesizes based on specific bodily DNA
Chains
298
composed of carbon, hydrogen, oxygen, and nitrogen
Amino acids