BIO130 Flashcards
Test Review
1
Q
Cell theory
A
Basic organizational unit, all organisms made of calls, cells come from pre existing cells
2
Q
Prokaryotic
A
No nuclei, single cell, bacteria and archaea
No membrane bound organelles, smaller, less DNA
3
Q
Eukaryotic
A
Nuclei, single/multicellular, plants, fungi, animal/human
Several membrane bound organelles, larger, chloroplast, cell wall, vacuole (1 storage, 1 like animal lysome)
4
Q
Origin of mitochondria
A
Originally free living aerobic prokaryotes able to use oxygen to generate ATP
E cubed model
5
Q
Ectosymbiosis
A
Symbiotic behaviour in which organisms live on body surface of another organism, can be internal
6
Q
E cubed model
A
Origins of mitochondria
Entangle, engulf, endogenize
Encloses endosymbiosis, endosymbiont escapes into cytosol and form into new compartment
7
Q
Origins of eukaryotes
A
Prokaryote > bacteria/archaea > mitochondria > single cell eukaryotes
Mitochondria and chloroplast have remnants of genomes, DNA, and membranes that signify derived from engulfed bacterial ancestor
8
Q
Endosymbiont
A
Cell living in cell with mutual benefit
9
Q
Model organisms
A
Living thing selected for intensive study as a representative of a large group of species
10
Q
Attributes of a model organism
A
-Rapid development with short life cycles
-Small size
-Readily available
-Tractability : ease of manipulation
-Understandable genetics
11
Q
Central dogma
A
Explanation of the flow of genetic information
12
Q
Genome
A
All DNA/DNA sequences in cell or organism
13
Q
Transcriptome
A
All RNA/RNA sequences in cell or organism
14
Q
Proteome
A
All protein/protein sequences in cell or organism
15
Q
Interactome
A
Protein-protein interactions in cell or organism
16
Q
Metabolome
A
Small molecule metabolites in cell or organism
17
Q
Phenome
A
All phenotypes in cell or organism
18
Q
Nucleic Acid
A
Genetic material in the cell
DNA: deoxyribonucleic acid
RNA: ribonucleic acid
19
Q
Nucleotide parts
A
1) Pentose sugar
-scaffold for base
2) Nitrogenous base
-varies
3) Phosphate group
-backbone
-1, 2, 3
20
Q
Base Types
A
Pyrimidine: 1 Ring
Purine: 2 Rings
21
Q
Pyrimidines
A
-Uracil
-Cytosine
-Thymine
“U C The PYRamids”
22
Q
Purines
A
-Adenine
-Guanine
“Al Gor stinks PU”
23
Q
DNA v RNA
A
Off the 2’ carbon RNA has oxygen DNA doesn’t
RNA: GCAU
DNA: GCAT, extra methyl group
24
Q
Nucleoside
A
Base+Sugar
25
Nucleotide
Base+Sugar+@ least 1 phosphate group
26
Nucleic acid chains
-DNA synthesized from dNTPs (deoxyribonucleoside triphosphate)
-RNA synthesized from NTPs (ribonucleoside triphosphate)
-Nucleotide linked by phosphodiester bonds
27
Interactions between individual molecules usually mediated by non covalent attractions
-Electrostatic attractions
-Hydrogen bonds
-Van Der Waals (Base stack)
-Hydrophobic force (Base ring structures)
28
Base Pairs
G-C bond
-3H bonds
-Stickier
A-T bond
-2H bonds
29
Complementary
Sequence of 2 strands
30
Denaturation
Destroy normal structure
31
Antiparallel
5’ > 3’ and 3’ > 5’
Double helix organized like this
32
5’
Phosphate group
-PO4
33
3’
Hydroxyl group
OH
34
Protein Structure: Primary
Amino acid sequence
35
Primary Structure: Secondary
Lots of examples
A helix
36
Protein Structure: Tertiary
3D structure
37
Protein Structure: Quaternary
More than 1 polypeptide chain
38
Protein Structure: Multi Protein Complexes
Multi protein complexes and molecular machines
39
Side chain/R group
Variable and determines the type of amino acid
Identify amino group, R group, carboxyl group, alpha carbon
40
Amino acid categories
-Acidic
-Basic
-Uncharged polar
-Nonpolar
41
Peptide bonds
-Occurs in the ribosome
-Condensation rxn
-OH off carboxyl: Carbonyl C
-H off another: Amide N
-Doesn’t change R group
-Backbone: everything except for R group
42
Alpha Helix
Could be entire polypeptide chain or just a small part
43
Alpha helix v DNA double helix
-R groups stick out : bases face inward
-R groups don’t support : base groups hold it together
-Single strand : double strand
-N and C end : 5’ and 3’ end
44
H Bonds: In atoms
Between carbonyl oxygen and amide hydrogen (peptide backbone)
45
H Bonds: Alpha helices
4 AA apart within same segment of chain (n-n+4)
46
H Bonds: Beta sheet
Between AA in different segments/strands of the chain
47
Coiled coil
Super secondary structure
-Helices do not have to create a coiled coil
-Amphipathic (define)
-Found in alpha keratin of skin, hair, and myosin motor proteins
-Helices wrap around each other to minimize exposure to hydrophobic AA R group to aqueous environment
48
Amphipathic
2 different biochemical/physical properties on different sides
49
Tertiary structure: held together by...
-Hydrophobic interactions
-Non covalent bonds
-Covalent disulfide bonds
-Other interactions among residue backbones and R groups
-Also between many helices and beta sheets
-How the rest of the polypeptide chain folds
50
Proteins fold into shape dictated by ________ but _______ help make the process more efficient and reliable in living cells
AA sequence
Chaperone proteins
51
Protein domains
-Often specialized for different functions
-Portion of protein that has its own tertiary structure, often semi independent structure
-Eukaryotic proteins often have 2 or more domains connected by intrinsically disordered sequences (Forming a larger overall tertiary structure)
-Important for protein evolution
-Src Protein Kinase
52
Protein families
-Have similar AA sequences and tertiary structure
-Members have evolved to have different functions
-Most proteins belong to families with similar structural domains
53
Quaternary Structure
Hemoglobin
-Formed from separate units/polypeptides 2a and 2B
-Sickle cell anemia, cause by mutation in B sub unit
54
Multi protein complexes
Many identical sub units
-Actin filaments
Mixture of different proteins and DNA/RNA
-Viruses and ribosomes
Very dynamic assemblies of proteins to form molecular machines
-machines for DNA replication initiation or for transcription
55
Studying proteins: Single or few
-Consider protein diversity
-Purify protein of interest (electrophoresis and affinity chromatography)
-Determine amino acid sequence
-Discover precise #D structure (x ray, crystallography, NMR spectroscopy, cryo electron microscopy, and AlphaFold)
56
Studying proteins: Large scale
-Identity/Structure
-Protein protein interaction
-Abundance/turnover
-Location in cell/tissue
57
Genome
All an organisms hereditary information
58
Base pair
Nucleotide pairs
59
Human genome
-3 billion base pairs per genome
-One genome from 1 parent and one from the other
-Standard human cell, 6 billion bp, 2 genomes
-20,000 protein coding genes
-50% repetitive DNA
-Less than 1% encodes protein
60
Genome size
-Does not equate to actual size
-Not always correlated with # of genes or organism complexity
61
Human genome: Unique sequences
-Non repetitive DNA in neither introns nor exons
-Protein coding exons: transcribed and translated
-Introns: transcribed not translated
ex. sequences that help cells determine with RNA to transcribe and how much
62
Human genome: Repeated sequences
-Segment duplication: thousands-hundreds of thousands bp
-simple repeats
-mobile genetic elements: sequences over long period of time cut themselves out, sometimes ate in
-DNA only transposon
-Retrotransposon: made into RNA
-LINEs: long interspersed nuclear element
-SINEs: short interspersed nuclear element (<500bp)
63
Packing DNA: Non packaged state
Small prokaryotic genome occupy considerable portion of cell volume
64
Packing DNA: Prokaryotes
-DNA condensed through folding and twisting
-Forms prokaryotic nucleoid
65
Packing DNA: Eukaryotes
Chromatin
-Tightly packed DNA must remain accessible for transcription, replication, repair
66
Florescence In Situ Hybridization (FISH)
Diagnostic technique for detecting presence of particular sequences
67
Chromosome
Single long linear DNA molecule and associated proteins (Chromatin)
68
Chromatin
-DNA double helix
-Beads on a string
.wrapped around protein
.nucleosome
-30nm fiber
.packed nucleosome
Loops
-Mitotic chromosome
.10,000 fold shorter than fully extended length
69
Nucleosome
-Chromatin isolated from cell in interphase
70
Core histones
-Connected by linker DNA
-DNA wraps 1 2/3 times
-Liner DNA can vary up to 80 nucleotide pairs long
-Middle contains 8 proteins
.rich in lysine and arginine, positive changes neutralizes DNA
-1 linker histone (H1)
.paper clip, clips DNA on
71
Nucleosome v. Core particle
-Core, H1, linker DNA
-no H1
72
Packing chromatin
-Specific clamp proteins and cohesins involved in forming chromatin loops
-Cells enter mitosis condensis replace cohesins to form double loops of chromatin to generate compact chromosome
-Packing/Unpacking requires ATP
73
Re-modelling chromatin
Chromatin modelling complexes and histone modifying enzymes are examples of proteins that change chromatin structure and alter access to DNA for replication or transcription
74
Heterochromatin
-Highly condensed chromatin
-gene expression is suppressed
75
Euchromatin
-Relatively non condensed chromatin
-Genes tend to be expressed
76
Transcription factories
Regions of the nucleus with lots of substrates and proteins for transcription
77
Conservative DNA replication
-Parent cell to daughter cells
-One cell has both parental strands one is entirely new
78
Semi conservative DNA replication
-One parent strand per new cell
-Always true in nature
79
Direction of DNA replication
-Bidirectional growth from starting point
-DNA is anti parallel
-New DNA 5' to 3'
-Template read 3' to 5'
-Replication fork
-Okazaki fragments
80
Replication fork
Origin of replication separate parent strands left and right
81
Origins of DNA replication
-Easy to open (A-T)
-Recognized by indicator proteins that bind t DNA
-Bacteria: single origin
-Eukaryote: multiple
-Replication fork is asymmetrical
-Leading strand replicated continuous, lagging is discontinuous
82
What do both eukaryotic and prokaryotic cells have
Ribosomes
83
What are some methods by which humans can be studied
-Cell cultures
-Clinical studies
-Organoids
84
On a molecular level it is possible that 2 prokaryotic species could be as different from each other as either is from eukaryotes
True
85
What organelles ancestor was likely engulfed by an early anaerobic eukaryote
Mitochondrion
86
Nomenclature for a nucleoside
Deoxycytidine
87
How many water molecules are created in the condensation rxn that creates a polypeptide chain from three amino acids
2
88
Why are alpha helices and beta sheets common folding patterns in polypeptides
Amino acid side chains are not involved in forming the hydrogen bonds, allowing many different sequences to adopt these folding patterns
89
______ bonds covalently link neucleotides together to make DNA or RNA while, ______ bonds covalently link together AA in polypeptides
Phosphodiester
Peptide
90
Extracellular proteins are directly exposed to extracellular conditions. To help maintain their specific 3D shape the polypeptide chains are often stabilized with ...
Disulfide bonds
91
Protein domains are often connected by relatively short lengths of polypeptide called ...
Intrinsically disordered sequences
92
Areas of the human genome that are not "protein encoding exons" include ...
DNA sequences that ensure transcription of the proper gene at the proper time, level, and space
93
A laboratory uses single stranded DNA probes with florescent dyes to detect the presence of cells infected with the human papillomavirus. This technique is known as ...
In Situ Hybridization
94
Chromosome duplication occurs during ____, starting at ____
Interphase
Origins of replication
95
Histone proteins pack DNA into a repeating arrat of DNA protein particles called ...
Nucleosomes
96
Okazaki fragments are found associated with the leading strand template
False
97
Primase is known as a ...
RNA polymerase
98
Enzyme telomerase solves the problem of replication at the ends of linear chromosomes by ...
Adding numerous short DNA sequences to the 3' end of the lagging strand template
99
Regarding double stranded DNA breaks, how are they caused, how can they be solved
Can be caused by radiation
Can be solved with non homologous end joining or homologous recombination
CANNOT repair by editing function of DNA polymerase
100
Copying errors not caught by the replication machinery can be corrected by ...
The DNA mismatch repair system
101
How does UV radiation from sunlight typically damage DNA
Promotes covalent linkage between 2 adjacent pyrimidine bases
102
How is transcription similar to DNA replication
Both processes depend on complementary base pairing of incoming nucleotides to a DNA template
103
mRNA represents the major class of non coding RNA
False
104
bacteria and eukaryotes do not require a primer to initiate transcription
True
105
While both bacterial and eukaryotic mRNA transcripts will have 3 phosphate groups at or near their 5' ends, only eukaryotic transcripts will also have a 7 mehtylguanosine attached there
True
106
Assembly of general transcription factors to a eukaryotic promoter begins at what sire in a promoter
The TATA box
107
What is absent in a properly folded tRNA
Thymidine dimers
108
Any given mRNA sequence has _____ possible reading frames, and the correct one is set by a _____
3
Initiation codon
109
Within the ribosome the formation of peptide bonds is catalyzed by ...
An RNA molecule in the large ribosomal subunit
110
Typically different aminoacyl-tRNA synthetases for every AA
True
111
Proteases that reside in the central cylinder of a proteasome are used to chop proteins into shorter peptides
True
112
What do initiator proteins bind to/do?
Bind to origin of replication
-destabilization of AT rich sequence
Helps helicase bind
-needs helicase loading protein
-Requires ATP
113
What can single strand binding proteins bond to?
What does this bonding do?
Where are the proteins?
-Stick to themselves after helicase, separates with binding ssDNA
-Stick back together after helicase, separates with binding ssDNA
-Prevents H bonding this way
-Single strand bonding proteins on leading lagging strand templates
114
RNA Primers Made by Primase
DNA polymerase requires bound primer
-Short sequence of nucleotides with free 3' OH
Primase synthesizes an RNA primer
-With free 3' OH that DNA polymerase can use
Primase 3'-5' along template strand
-Synthesizes 5'-3' (Adds to 3')
-Primase + Helicase = Primosome
115
DNA Polymerase
Incoming deoxynucleoside triphosphate pairs with base in template
-DNA polymerase catalyzes covalent linkage of deoxynucleoside triphosphate into new strand
-Read 3'-5'
116
What does a sliding clamp do?
Holds the DNA polymerase on the newly synthesized strands
117
How are okazaki fragments on lagging strands linked together?
-DNA polymerase adds nucleotides to 3' end of new RNA primer to synthesize new okazaki fragments
-Previous RNA primer removed by nucleases and replaced with DNA by repair polymerase (Gaps are called Nicks)
-Nick sealed by DNA ligase (covalent bond)
118
Replisome
-Type of molecular machine
-All proteins in DNA replication working together
119
Leading strand synthesized continuously from ______
Single RNA primers
120
Lagging strand synthesized discontinuously from ______
Multiple primers
121
Okazaki fragments are made of
RNA primer and DNA
122
What happens as DNA is unwound
DNA double helix want to spin
-Unable to spin due to space
-Twists around itself, super coil + torsion
-problem in circular chromosomes and larger linear eukaryotic chromosomes
123
What is the solution to super coils due to DNA spinning?
Topoisomerase
-Cuts 1 of 2 strands to unwind then reseals the Nick
-Transient single strand break
124
What happens at the end of eukaryotic linear chromosomes during replication?
Lagging strand has issues
-Primase isn't good at putting a primer at the very end
-Where it does put the primer it needs to be removed
-After removal left with 5' ends DNA cannot add to
-Incompletely replicated: loss of sequence information
125
How can we fix issues with the lagging strand at the end of eukaryotic linear chromosome replication?
Telomerase
-Repetitive sequence added to 3' end of parent strand
-Has RNA template, bp with DNA
-Adds more DNA on 3' end then releases and re-binds further up (G rich end)
-Completion of lagging with DNA polymerase
126
Telomerase and Cancer
-Telomerase is abundant in stem and germ line cells not somatic
-Loss of telomerase limits number of rounds of cell division
-Most cancer cells produce high levels telomerase
127
Finding and Correcting Mistakes: 3' to 5' exonuclease repair
-Backspace
-Removes misincorporated nucleotide
-DNA polymerase has editing sit
128
Finding and Correcting Mistakes: Standard directed mismatch repair eukaryotes
-If proofreading fails
-Initiated by detection of distortion in geometry of double helix generated by mismatched base pairs
-MutS protein recognizes and locks onto DNA mismatch
-MutL scans DNA (Sliding clamp:strand with nick)
-MutL nuclease activated + initiates strand removal
129
Finding and Correcting Mistakes: Prokaryotes
-Typically don't detect nicks
-Detect methylated adenines
-New strand doesn't have them
130
After synthesis DNA can still be damaged, how?
Pyrimidine dimer
-Covalent bonds between bases, messes up locations
Spontaneous damage
-Water with wrong nrg, wrong place/time, bumps into purine and goes through depurination
Spontaneous damage
-Water, bumps into cytosine turns uracil, deamination
131
How do we fix double stranded breaks?
Non homologous end joining
-Break repaired with loss of neucleotides at repair site
Homologous recombination
-Recombination specific nuclease (trim) but use other strand as template
132
Molecular definition of a gene
Genes are segments of DNA that are transcribed into RNA
133
What does RNA do? How does it function?
-RNA can encode for protein
-RNA functions as RNA and may not need to be translated into protein
-More mRNA means more of that protein
134
Ribonucleotides
-Ribonucleotides triphosphates used (ATP, UTP, CTP, GTP)
-RNA is made antiparallel and complementary to DNA
-RNA is made in the 5' to 3' direction adding to the 3' end
-DNA template read 3' to 5'
135
RNA Transcript
-ssDNA template
-Phosphodiester bonds
-Base pairing
136
Transcription Cycle
-Sigma factor binds to RNAP ad fins promoter sequence
-Binds to core enzyme to form holoenzyme
-Localized unwinding of DNA, few short RNAs synthesized initially and then RNAP clamps (Abortive transcription: Copy 1st 10) down sigma factor released
-Elongation
-Termination and release of RNA
-NO primer
137
Promoter Sequence
-Sigma factor binds to this
-We call the promoter what the factor binds to and the in between
-1st pair +1 on DNA (nucleotide #)
-Higher # downstream
-Promoter consensus sequence shown (-10, -35)
138
Eukaryotic transcription is more complex
True
139
Transcription Initiation
-mRNA, rRNA, and tRNA
-Eukaryotes have a few more RNAs including temolerase, snRNA (splicing of pre mRNA), and miRNA (block translation causeing degradation)
-Eukaryotic RNA polymerase
.each RNAP is a multi subunit protein
.responsible for transcription of different RNA
.1: rRNA
.2: mRNA (protein coding genes) miRNA
.3: tRNA, 5s rRNA
140
Eukaryotic II v. Bacterial RNAP
Bacterial
-5 sub units
-Sigma subunit: similar function transcription factor
Eukaryotic II
-12 sub units
-Special carboxyl terminal domain (CTD)
-Require proteins to help position @ promoter (Transcription factor)
-Need to deal with chromosomal structure
141
Eukaryotic Promoters
-More variable than bacterial
-1 or more specific sequences called elements
-Elements @ specific locations
-Elements recognized by specific general transcription factors which help position RNAP
142
TATA Box
-30 base pairs upstream from start site of transcription
-Helps position RNAPII and general transcription factors
-Binding of TATA binding protein sub unit of transcription factor II in minor groove
-Mobilizes binding of TFIIB complex adjacent TATA box
-Other transcription factors bind
-RNAP II with other TFs will bind in correct orientation and transcription start site
-Helicase activity and phosphorylation of CTD of RNAP II
-Enhancer sequences with activation proteins, activates mediator, activates protein
143
Phosphorilate
Add phosphate group to S (Ser) located by the CTD
144
C Terminal Domain
-Tandem repeats of 7AA
145
mRNA Processing
-Coupled with transcription
-Phosphorylation of C terminal tail resulting in binding of RNA processing proteins and additional phosphorylation of CTD, including Ser 2
146
mRNA Processing: Capping
-Helps protect RNA from exonucleus
-Completed before mRNA fully transcribed
-Cap has triphosphate bridge (2 5' ends) exonuclease cannot cut it, too weird
-7 methylguanosine
147
mRNA Processing: Splicing
-Splicesome
-Branch point A attack 5' splice site
-Adenine from phosphodiester bond between 2' and 5' of intron
-3' of one exon reacts with 5' of next exon to release intron
-Pre mRNA cant self splice
-Splicesomes have snRN bound to protein
-Splicing complete: exon junction complex added
148
mRNA Processing: Abnormal Splicing
-Exon skipping
-Activated cryptic site
-New exon
149
mRNA Processing: Consensus Sequence + 3' End Modifying Proteins
-After transcribed 3' end processing proteins recognize and are recruited to mRNA
-Poly A sequence is not encoded in the genome
-Consenses sequence direct cleavage and polydenylation to 3'
-3' processing proteins move from CTD to mRNA
-Result: mature mRNA
150
mRNA Export
Move mRNA to cytosol (Protein synthesis)
-Cap binding proteins
-Poly A binding proteins
-Exon junction complexes: Semi optional, some mRNA don't get spliced
151
Reading Frames: Translation
Define amino acid sequence
-5' most AUG, read 3 nucleotides at a time
152
Nucleotide Pair Substitution
Silent
-Same amino acid created
Missense
-Different amino acid created
Nonsense
-Stop codon
153
tRNA: Translation
-Recognizes the codon on mRNA and brings the proper amino acid
-About 80 nucleotides long
-5' and 3' ends, transcribed as per usual
-Base pairs with itself in regions, making double helicase regions
-3' end is where the AA gets attached
-Anticodon binds to mRNA codon, antiparallel and complementary
-Modified bases
154
Genetic Code
-Reads as mRNA triplets
-Encoding all 20 amino acids
-Redundancy: Multiple codons for the same amino acid
155
How do we manage redundancy in the genetic code?
-More than 1 tRNA for many amino acids
-Some tRNA can recognize and base pair with more than 1 codon (Wobble)
156
Explain the Wobble Position
-Manages redundancy
-3' of codon and 5' of anticodon
-Many anticodon bases for the wobble codon base (Variety)
-There's rules
-Bacteria is more flexible than eukaryotes
-I: Inosine
157
How do we ensure fidelity?
-Aminoacyl-tRNA synthase recognizes tRNA and put the proper AA
.identify tRNA anticodon nucleotides, recognizes nucleotide sequences of 3' end, reading nucleotide sequences at additional positions
-Base pairing
158
Where are ribosomes found and how are they built?
-On endoplasmic reticulum or in cytosol
-Has large and small sub units
.Large: many protein, many rRNA
.Small: many protein, one rRNA
159
Large Sub Unit Sites: Ribosomes
A: aminoacyl
P: peptidyl
E: exit
160
Overview of Translation
-NRG in AA and tRNA bond in P site make peptide synthesis energetically favorable
-Peptide bond formation catalyzed by peptidyl transferase activity of rRNA in large sub unit
161
Ribozyme
-RNA molecules that posses catalytic activity
-RNA catalyzes peptide bond
162
EF
Elongation factor
163
EF-Tu
EF1 in Eukaryotes
-Checks aminoacyl tRNA
-Goes to A cite checks for proper base pairing
.If base pairing isn't correct EF-Tu is not released and the peptide bond cannot form, the entire thing is cut off
.If base pairing is correct GTP is hydrolysed and EF-Tu is released
164
EF-G
EF2 in Eukaryotes
-Helps ribosome move the small sub unit forward 1 codon and helps speed up elongation of polypeptide chain
165
Initiation of Translation: Prokaryotes
-Shine Dalgomi sequences on mRNA base pair with rRNA in small ribosomal subunits
-Positioning of small subunits to initiating AUG codons on mRNA also requires initiation factors (IF)
-fMethionine aminoacyltRNA binds to initation codon
-Large ribosomal subunits bind
166
Initiation of Translation: Eukaryotes
-Small ribosomal subunit with tRNA + Met, no mRNA yet
-Find 5' end looks for AUG, binds
-Large ribosomal subunit comes in
167
Translation: Termination
Protein recognizes stop codon, not tRNA
168
Translation: Polyribosomes
Chain of ribosomes all translating one after the other
169
Translation: Protein Folding
Chaperone proteins
Hsp 60 and 70
170
Post Translational Modification
Many proteins require
-phosphorylation
-glycosylation
Covalent modifications may be required to
-make protein active
-recruit protein to correct membrane and organelle
171
How is protein degradation controlled?
Proteins tagged for degradation
-Small proteins called ubiquitin covalently attached directs them to the proteasome where they are degraded by proteases
172
Antibiotics
-There are many inhibitors that act only on bacteria
-A lot of antibiotics screw up bacterial translation
-Not antibiotic its poison, acts on eukaryotes
173
Beta Sheet
-H bonding between carbonyl oxygen, 1AA, and amide hydrogen of the AA in neighboring strand
-R group is not involved and alternate up and down
-Typically 4 or 5 strands parallel or anti parallel
174
How is genetic code organized?
-Polar, nonpolar, charges, uncharged
-Groups of amino acids with similar properties
175
Cysteine
-Disulphide bonds
-R group CH2SH
-S of the R group forms inter or intro disulphide bonds due to oxidization
-helps brace the structure
-Redox: in cytosome, no bonds, breaking bonds
