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Midterm PHGY 170 > Midterm > Flashcards

Midterm Flashcards

1
Q

First tenet

A

All living organism are composed of one or more cells

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2
Q

Second tenet

A

The cell is the basic unit of structure and organization in organisms

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3
Q

Third tenet

A

All cells come from pre existing cells

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4
Q

What are the two basic cell types

A

Prokaryotic and eukaryotic

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5
Q

Prokaryotic nucleus

A

No true nucleus or any membrane bound organelle

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6
Q

Prokaryotic cell size

A

Smaller cell (1-5um)

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7
Q

Prokaryotic amount of cells

A

Always unicellular

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8
Q

Prokaryotic cell division

A

Binary fission

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9
Q

Prokaryotic reproduction

A

Always asexual

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10
Q

Type of prokaryotic cells

A

E.coli

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11
Q

Eukaryotic nucleus

A

Had a nucleus and membrane bound organelles

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12
Q

Eukaryotic cell size

A

Large cell (10-30um)

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13
Q

Eukaryotic amount of cells

A

Usually multicellular

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14
Q

Eukaryotic cell division

A

Mitosis/meiosis

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15
Q

Eukaryotic reproduction

A

Sexual or asexual

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16
Q

Types of eukaryotic cells

A

Plants and animals

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17
Q

Types of cells found in human body (8)

A

Muscle
Nerve
Connective tissue
Bone
Secretory
Adipose
Epithelial
Red blood cell

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18
Q

Epithelial cell function

A

Form protective barrier in tissue and may be specialized to absorb or secrete compounds

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19
Q

Muscle cell function

A

Are responsible for movement of the skeleton, heart and many organs. These are specialized structures and proteins that allow them to generate motion

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20
Q

Nerve cell function

A

Conduct electrical signals throughout the body, control the contraction of muscles, and are responsible for senses including taste, touch, smell, sight and hearing

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21
Q

Connective tissue cell function

A

Create extracellular material that holds cells together in tissue.

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22
Q

Bone cell function

A

Form the bones of the skeletal system that give strength and support to the body

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23
Q

Secretory cell function

A

Form glands and secrete substance ie hormones enzymes

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24
Q

Adipose cell function

A

Are located throughout the body to store fat. Fat in the form of triglycerides which are released when the body is in a period of fasting

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25
Q

Red blood cell function

A

Are cells formed in bone morrow and released into circulation where they move and deliver oxygen throughout body

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26
Q

Eukaryotic cell structures

A

Plasma membrane
Nucleus
Mitochondria
Endoplasmic reticulum
Golgi apparatus
Cytoskeleton
Endosomes
Lysosome

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27
Q

What is the plasma membrane

A

Is like the city limit and border police. It is semi permeable phospholipid bilaterally that keeps all of the cells organelles contained and regulates what cane come in or leave

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28
Q

What is the nucleus

A

Is the leader of the cell, makes the law. the nucleus stores these law in the dna and protects it

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29
Q

What is the mitochondria

A

Are the power plants of eukaryotic. They produce energy for the cell to use in all of its processes in the form of ATP

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30
Q

What is the endoplasmic reticulum

A

Acts as a highway system, carrying molecules around the cell and as a factory warehouse that makes lipids and proteins and stores ions

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31
Q

What is the Golgi apparatus

A

Is the post office of the eukaryotic. That processes and packages proteins then sends them across the cell

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32
Q

What are endosomes, lysosomes

A

Some smaller membrane bound organelles contain specific proteins and enzymes.

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33
Q

What do endosomes do

A

Are the waste collection vehicles that sort and start breaking things down

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34
Q

What do lysosomes do

A

Are recycling plants that break down proteins, lipids, and nucleic acid

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35
Q

What do peroxisomes do

A

Deal with hazardous waste such as hydrogen peroxide

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36
Q

What is the cytoskeleton

A

Is the steel girdles holding building together. Actin, microtubles and filaments stabilize memodeformations

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37
Q

What are the two building blocks of a cell

A

Carbon and water

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38
Q

What is polarity

A

Polar properties of water make it an excellent solvent. This facilitates the delivery of nutrients and removal of wastes

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39
Q

What is heat capacity

A

The high specific heat capacity of water allows for thermoregulation by acting as a heat sink for many chemical reactions that occur within a cell

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40
Q

What is carbon

A

Is the building block to all life. It is small and can form up to four covalent bonds

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41
Q

Four carbon based molecules

A

Benzene, pyridine, cyclopentane, cyclohexane

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42
Q

What are lipids

A

Are the building blocks of oil and fats. They are made up of hydrocarbon chains and often insoluble in water

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43
Q

What is amphipathic

A

A molecule that is both hydrophilic and hydrophobic

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44
Q

What are three common lipids

A

Cholesterol
Phospholipids
Triglycerides

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45
Q

What is cholesterol

A

Regulates cell membrane fluidity and is a biological precursor for compounds such as steroid hormones, bile acids and certain vitamins

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46
Q

What are phospholipids

A

Are amphipathic lipids that form cell membranes. Have a hydrophilic head and a hydrophobic tail

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47
Q

What are triglycerides

A

Are the main component of body fat used to store energy

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48
Q

What are carbohydrates

A

Classified as mono, di, oligo, polysaccharides

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49
Q

What is monosaccharides

A

Are single carbohydrate molecules containing only carbon hydrogen and oxygen. Ie glucose

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50
Q

What is disaccharides

A

Are two monosaccharides bonded together connected by a glysosdic bond. Ie sucrose

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51
Q

What is oligosaccharides

A

Are composed of three to ten monosaccharides linked together. Ie raffinose

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52
Q

What is a polysaccharides

A

Are much longer chains, are even more complex, and play many important roles in the cell. Ie glycogen

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53
Q

What is nucleotides

A

Are the building blocks of nucleic acids like dna and rna

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54
Q

What does DNA stand for

A

Deoxyribonucleic acid

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55
Q

What does RNA stand for

A

Ribonucleic acid

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56
Q

What are amino acids

A

Are the building blocks of peptides and proteins

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57
Q

The carboxylic group

A

Can also exist as a negatively charged carboxylate

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58
Q

The r-group amino acid

A

Is unique to each amino acid and gives it its distinct molecular characteristics

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59
Q

Types of R-group amino acids

A

Hydrophobic amino acid
Charged hydrophilic amino acids
Polar amino acids
Aromatic amino acids

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60
Q

What is a hydrophobic amino acid

A

Also called nonpolar. Normally found in the core of the protein or interacting with fats and lipids

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61
Q

Hydrophobic: aliphatic

A

The R-group consist of carbon chains which can be straight, branched, or non-aromatic rings. Ie glycine, alanine valine

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62
Q

Hydrophobic: aromatic

A

The R-group contains an aromatic rings that has double bonds similar to benzene

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63
Q

What is charged hydrophilic amino acids

A

Carry a positive or negative charge. Location of charge found on the outside of proteins they interact with water. Ie lysine, arginine

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64
Q

What are polar amino acids

A

Can form hydrogen bonds that stabilize proteins. They are common in the outside of a protein. Ie serine, tyrosine

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65
Q

What is cysteine

A

Has a sulfur containing thiol that can form a covalent bond. These are significant for forming and maintaining three dimensional protein structures

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66
Q

What are aromatic amino acids

A

Ring structures with double bonds that have distinct properties associated with this chemical structure. They are very large

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67
Q

What are amphipathic amino acid

A

Having both hydrophilic and hydrophobic parts

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68
Q

What are peptides

A

A short chain of amino acids connected together to form peptide bonds

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69
Q

What are proteins

A

Made up of long chain amino acids 20 plus called polypeptides

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70
Q

what is a genome

A

The complete set of genetic material in an organisms aka all DNA in cell

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71
Q

What are genes

A

A sequence of nucleotides in DNA that determines certain characteristics

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72
Q

What is DNA held by

A

Phosphodiester bonds

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73
Q

What is the structure of a nucleotide

A

Five carbon sugar
Phosphate group
Nitrogenous base

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74
Q

What is the phosphate group

A

Attach to the 5 or 3 carbons

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75
Q

What is nitrogenous base

A

Two categories of bases: purines and pyrimidines. Attach to 1 carbon of sugar in a single nucleotide

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76
Q

What are purines

A

Have two rings in their structure: adenine and guanine

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77
Q

What is pyrimidines

A

Only have one ring in their structure:
Cytosine and thymine (DNA)
Uracil (RNA)

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78
Q

What does adenine pair with

A

Thymine

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79
Q

What does guanine pair with

A

Cytosine

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80
Q

What is a double stranded helix

A

DNA becomes a double stranded helix when bases comes into little contact of water creating a spinal staircase

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81
Q

What is RNA

A

A nucleic acid plays a critical role in synthesis of proteins

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82
Q

RNA structural differences to DNA

A

Nucleotides in RNA contain ribose rather than dexyribose.
RNA single stranded and is less stable then DNA

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83
Q

RNA functions and types

A

Messenger RNA
Transfer RNA
Ribosomal RNA

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84
Q

What is messenger RNA

A

Carrie’s instructions for making proteins in the cell

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85
Q

What is transfer RNA

A

Brings amino acids for protein synthesis during translation

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86
Q

What is ribosomal RNA

A

In charge of translating RNA into protein

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87
Q

What are Exons

A

Coding DNA contains information that is used to make protein

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88
Q

What are introns

A

Non-coding DNA not used to make protein

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89
Q

What is regulatory sequences

A

Control when a gene is turned on or used

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90
Q

Processes need for information to be converted from DNa to protein are?

A

Replication
Transcription
Translation

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91
Q

What is replication (DNA)

A

DNA is replicated before a cell divides so that both the original cell and the new daughter cells each have a complete copy of DNA (enzyme involved polymerase)

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92
Q

What is transcription

A

Information from a section of the DNa is transcribed into RNA to transport this information out of the nucleus for protein production (enzyme involved is RNA polymerase)

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93
Q

What is translation (RNA)

A

RNa is read and translated from nucleotides to amino acids to produce proteins that perform a specific function in the cell (enzyme used ribosome)

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94
Q

What are the three major stages of DNA replication

A

Initiation
Elongation
Termination

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95
Q

DNA: initiation of replication

A
  • Double stranded DNA needs to be separated into single strands
  • protein in binding
  • DNA unwinding
    -RNA Primers
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96
Q

DNA: initation of replication (protein binding

A

A group of proteins binds to the ORC to begin replication (most important DNA helicase)

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97
Q

DNA: initation of replication (DNA unwinding)

A

DNA helicase unwinds DNA into two single strands called the replication fork. This is where replication occurs

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98
Q

DNA: initation of Replication (RNA Primers)

A

Each single strand will act as template for synthesis for new strands

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99
Q

DNA stage two: elongation

A

Primers are elongated by DNA polymerase

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100
Q

DNA stage two: elongation (direction)

A

DNA polymerase can only add nucleotides to the 3 end of dna thus meaning it can only move along parent strand dna in a 3 to 5 direction

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101
Q

DNA stage two: elongation (catalysis)

A

The new phosphodiester bonds between an incoming nucleotide and existing in the backbone

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102
Q

DNA stage two: elongation (leading strand)

A

Runes 3 to 5 direction along parent strand

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103
Q

DNA stage two: elongation (lagging strand)

A

Built 5 to 3 direction running away from replication fork

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104
Q

DNA stage three: termination

A

A stretch of dna can’t be replicated. Causing an over hang

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105
Q

DNA stage 3: termination (overhang)

A

To prevent shortening of chromosomes telomeres are added which are long non coding ends of each chromosomes

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106
Q

RNA polymerase

A

Synthesis of RNA from dna is facilitated by this enzyme

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107
Q

RNA polymerase I

A

Is responsible for synthesizing most of the rRNA required for a functional risbosome

108
Q

RNA polymerase II

A

Synthesizes messenger RNA

109
Q

RNA polymerase III

A

Synthesizes transfer RNA as well as some other RNA molecules

110
Q

RNA transcription three mechanisms

A

Guiding RNA pol II to correct strand
Unwinding DNA
Phosphorylating RNA pol II

111
Q

Three post transcriptional RNA

A

5 methylguanosine cap
3 polyadenylation
Splicing

112
Q

RNA 5 methylguanosine cap

A

Occurs shortly after mRNA synthesis to protect mRNA molecule from premature degradation by nucleases

113
Q

DNA and RNA replication occurs in

A

Nucleus for both

114
Q

DNA and RNA product

A

DNA: replication of DNA
RNA: RNA made from one or few genes

115
Q

DNA polymerase involvement

A

DNA: dna polymerase
RNA: RNA poll II

116
Q

Codons

A

Important to know they are three nucleotides long

117
Q

Main components of translation

A

MRNA
Protein factors
TRNA
Ribosome

118
Q

MRNA

A

Is delivered along with some protein from nucleus to the cytoplasm

119
Q

Protein factors

A

Help the small ribosomal subunit identify the initiation site

120
Q

tRNA

A

To deliver the correct amino acid to a growing peptide

121
Q

Ribosome

A

Composed of large and small subunit
Small: is responsible for binding to mRNA
Large: has three important sites A P E

122
Q

Factors that can damage DNa

A

UV light
Oxidation
DNA strand breaks

123
Q

Four types of DNA mutations

A

Point of mutations
Insertion
Deletion
Large scale deletion, insertion, recombination

124
Q

Point of mutation

A

A single nucleotide is changed resulting in one of three outcomes
Silent mutation
Missense mutation
Nonsense mutation

125
Q

Silent mutation

A

Does not cause amino acid to change

126
Q

Missense mutation

A

Does cause the amino acid to change

127
Q

Nonsense mutation

A

Replaces an amino acid codon with a stop codon ending translation and preventing the production of the rest of the amino acid

128
Q

Insertion mutation

A

An extra base pair is added to DNA which alters every amino acid produced

129
Q

Deletion mutation

A

Base pair or more is removed from DNA sequence

130
Q

Nuclear envelope

A
131
Q

Nuclear pores

A

Allows large molecules to enter and exit the nucleus

132
Q

Nucleoplasm

A

Contains nuclear nutrients and a network of filaments provides organization to the DNA

133
Q

Chromatin

A

Is a complex of DNA and proteins forming highly organized fibres and is located in different defined areas of the nucleus

134
Q

Chromosomes

A

Are highly condensed chromatin found in the nucleus only during cell division

135
Q

Nucleolus

A

Organizes chromatin for genes that encode rRNA production site for ribosomes

136
Q

Nuclear matrix

A
  • helps to organize chromosomes into compartments
  • helps maintain structure of nucleus
137
Q

Function of nucleus

A

Protects DNA

138
Q

DNA packaging

A

Helps package DNA carefully into nucleus

139
Q

5 levels of DNA PAckaging

A

The DNA double helix
nucleosomes
Chromatin fibres
Chromatin looped domains
Heterochromatin

140
Q

Nucleosomes

A

Known as Beads on a string
DNA wrapped twice around protein called histones shorting DNA

141
Q

Chromatin fibre

A

Involves the string of nucleosomes coiled into a spiraling fibre

142
Q

Chromatin looped domains

A

The 30-40um chromatin fibre made of nucleosomes is formed into loops with an average length of 300um

143
Q

Heterchromatin

A

The folded looped domains formed by DNA are further compressed and folded

144
Q

The endomembrane system consists of

A

Rough ER
Smooth ER
Golgi apparatus

145
Q

Endomembrane system function

A

Process the transport of cargo throughout the cell

146
Q

Exocytic pathway

A

The process of moving cargo out of the cell

147
Q

Endocytic pathway

A

The process of moving cargo into cell

148
Q

The endoplasmic reticulum

A

Is made up of organized flattened disks of the membrane called cisternae

149
Q

Cytosol

A

A fluid contained by the plasma membrane of the cell

150
Q

Rough ER

A

Is the site for protein translation and some protein modifications

151
Q

Smooth ER

A

Does not have ribosomes on it and is responsible for lipid processing, carb metabolism and can store calcium

152
Q

Calcium regulation

A

Regulates calcium ion concentration in muscle cells which is important for muscle contraction

153
Q

Transport vesicles

A

Proteins that have been made in the ER are shuttled in transport vesicles to Golgi apparatus for further modifications

154
Q

Golgi apparatus

A

Is involved in both protein modification and transport. Acts as post office, labels and sorts proteins and directs them to their final destination

155
Q

Three regions of the Golgi apparatus

A

Cis Golgi network
Medial Golgi network
Trans Golgi network

156
Q

Cis Golgi network

A

Receives proteins from the ER that have entered the endomembrane pathway

157
Q

Medial Golgi network

A

Sugar groups called oligosaccarides can be added to proteins

158
Q

Trans Golgi network

A

Performs the final packaging to send materials to different organelles and sorts cargo to specific destinations

159
Q

Tran Golgi network levels

A

Other organelles
Retrograde transport
The lysosomes
Cargo transport

160
Q

Trans Golgi network: other organelles

A

The cell needs to deliver the correct proteins to organelle
Packages these product to go to their final location

161
Q

Trans Golgi network: retrograde transport

A

Some proteins that have arrived from ER contain ER retention signal

162
Q

Trans Golgi network: the lysosome

A

M6P is added

163
Q

Trans Golgi network: cargo transport

A

Transport of vesicles to the outside of the cell is accomplished by exocytosis

164
Q

Endosomes

A

Hold content coming into the cell from the extracellular space. They help sort cargo

165
Q

Lysosomes

A

Involved in waste disposal break down proteins lipids

166
Q

Perixisomes

A

Break down molecules specifically those that generate hydrogen peroxide as a byproduct

167
Q

Lumen

A

Is the interior space of a tubular structure

168
Q

4 steps of translocation proteins into ER

A

Signal sequence
SRP binding
ribosome docking
Translocation

169
Q

Translocation proteins ER: signal sequence

A

Transport of proteins into the ER begins during translation this is accomplished by the presence of signal that translated as part of the protein

170
Q

Translocation proteins ER: SRP binding

A

As it emerges from the ribosome interacts with receptor. These bind to the ribosome that translating the protein

171
Q

Translocation of proteins ER: ribosome docking

A

During the pause in translation the ribosome docks onto the ER membrane by the SRP interacting with an SRP receptor

172
Q

Translocation of proteins ER: translocation

A

Restarts and once the proteins has translocated into the ER

173
Q

Transmembrane domain

A

The translocation for transmembrane proteins recognizes a signal that is similar to the ER signal sequence

174
Q

Enzymes involved in post translational modification

A

Protein disulphide
Binding protein chaperone

175
Q

Protein disulphide

A

They help form disulfide bonds between the thiol group I. The side chains of the cysteines. Helps protein to fold and stabilize

176
Q

Binding protein chaperonins

A

Help fold the polypeptide by binding hydrophobic patches in recently translated proteins

177
Q

Formation of peptide bonds

A

Carboxylic acid group of one amino acid and the amino group of a second amino acid undergo dehydration

178
Q

Protein structure hierarchy primary

A

Is a linear peptide sequence starts at amino acid terminal end of peptide and concludes at the carboxy terminus

179
Q

Protein hierarchy secondary

A

Are the region of organization in the peptide sequence

180
Q

Protein hierarchy secondary: alpha helix

A

Is a tight coil that forms hydrogen bonds between the backbone of every fourth amino acid

181
Q

Protein hierarchy secondary: beta sheets

A

Are planes that are formed between rows of amino acids with hydrogen bonds between the backbones

182
Q

Protein hierarchy tertiary

A

Is the 3D structure of a complete protein

183
Q

Protein hierarchy quaternary

A

Is when multiple proteins are assembled into a complex ex hemoglobin

184
Q

Domains

A

Is the basic building block of protein structure. Can be composed of 20 or more amino acids

185
Q

What defines shape and function of protein

A

PH
Temperature
Ions such as calcium or magnesium

186
Q

Two major types of modifications

A

Covalent mod (long lasting)
Noncovalent mod (short lived)

187
Q

Plasma membrane

A

is made up of phospholipids which form double layered sheets

188
Q

Semi permeable

A

Means that some molecules may cross while other cannot

189
Q

Hydrophobic

A

Molecules sand small neutral molecules can freely diffuse through

190
Q

Polar organic

A

Molecules ions and proteins cannot diffuse through a membrane

191
Q

Phospholipids

A

Are independent entities and do not form polymer rather they are separate molecules that cluster together to form structures such as membranes

192
Q

Phospholipids are composed of four major components

A

Head group
Phosphate group
Glycerol
Two fatty acid tails

193
Q

Phospholipids: head group

A

Attached to phosphate group and its chemical properties determine where the phospholipid ends up in the cell

194
Q

Phospholipids: phosphate group

A

The hydrophilic charged component of the phospholipids

195
Q

Phospholipid: glycerol

A

Is a three carbon chain with three hydroxyl groups it acts as the backbone of the phospholipid

196
Q

Phospholipids: fatty acid tail

A

Two long hydrocarbon chains which can vary in composition and bond. Attach to the glycerol backbone

197
Q

The six major types of phospholipid head groups

A

Polar: phosphatidyl-inositol (PI), phosphatidyl-glycerol (PG)
Cardiolipin (CL)

Charged: phosphatidyl-serine (PS), phosphatidyl-ethanolamine (PE)
Phosphatidyl-choline (PC)

198
Q

Other classes of lipids

A

Cholesterol
Glycolipids
Sphingonyelin

199
Q

Cholesterol

A

Major membrane component in tissues. Key component has hydroxyl group on one of its rings

200
Q

Glycolipids

A

Are also common in membranes and have sugar carbohydrate group attached to the lipid. Often involved in cell to cell signalling

201
Q

Sphingonyelin

A

Another common component in cell membranes. Found wrapping around axons of nerve cells

202
Q

Sphingolipids

A

Consists of phosphcholine head group, phosphate group, sphinosine and a fatty acid

203
Q

Phospholipids clusters

A

Spontaneously to maximize hydrophobic and hydrophilic interactions can reform easily and does not require high amounts of energy

204
Q

Four major types of phospholipid cluster

A

Micelles
Liposomes
Monolayer
Bilayer

205
Q

Micelles and liposomes

A

Surrounded by polar water phospholipids will form either droplets with fatty acid tail in center (micelles) or tight bolsters with hollow middle (liposomes)

206
Q

Monolayer

A

At the boundary of water and atmosphere phospholipids will form a single layer with the polar head groups pointed down into the polar h2o

207
Q

Bilayer

A

In cells phospholipids form bilateral with the polar head groups pointed out towards the aqueous environment inside and outside the cell

208
Q

Cytoplasmic leaflets

A

Leaflets facing the cytoplasm

209
Q

Exoplasmic leaflet

A

Leaflets facing the exterior of the cell

210
Q

Types of transporters

A

Floppases
Flippases
Scrambalases

211
Q

Floppases

A

Keep most PC, sphingomyelin and cholesterol in the exoplasmic leaflet (to flop out)

212
Q

Flippases

A

Keep most PS, PE, PI in the cytosolic leaflet (to flip in)

213
Q

Scramblases

A

Briefly disrupt membrane asymmetry by randomizing phospholipids

214
Q

Gradients

A

As an increase or decrease of the magnitude of property from one point to another

215
Q

Osmotic gradients

A

Difference in concentration of molecules between one side and other side leads to osmotic pressure

216
Q

Aquaporins

A

Are channels that have a hydrophilic interior to allow water to move through the plasma membrane

217
Q

Three classifications of tonicity

A

Hypertonicity
Isotonicity
Hypotonicity

218
Q

Hypertonicity

A

Solution has greater amounts of solute outside of the cell than inside. Causing water to flow out of the cell. This causes the cell to lose volume

219
Q

Isotonicity

A

Solution has equal amounts of solute inside and outside of the cell. The ideal state for a cell

220
Q

Hypotonicity

A

Solution has lower amounts of solute outside the cell than inside. Causing water to flow in. This makes the cell swell

221
Q

Fluid mosaic

A

Proteins reach membrane

222
Q

Types types of revised fluid mosaic model

A

Membrane constituents
Hydrophilic groups

223
Q

Fluid mosaic: membrane constituents

A

Phospholipids proteins can join together to form complexes in the membrane

224
Q

Fluid mosaic hydrophilic groups

A

Hydrophilic head groups of phospholipids can interact with hydrophilic portions of the membrane proteins.

225
Q

Lipid raft

A

Is a cluster of membrane proteins, phospholipids and other membrane constituents forming distinct patches that are chemically and physically distinct from the surrounding membrane

226
Q

Factors affecting membrane fluidity

A

Temperature
Lipid content
Cholesterol content
Protein content

227
Q

Membrane fluidity: temperature

A

Increase the motion in the membrane increase making it more flexible. Cooler temps cause the membrane to become more rigid

228
Q

Membrane fluidity: lipid content

A

The length of lipid chains influences the rate of movement of the plasma membrane. Shorter lipids move more compared to longer chains

229
Q

Membrane fluidity: cholesterol content

A

Is rigid bulky and hydrophobic and thus acts as a spacer in lower concentrations making a membrane more fluid. Higher concentrations will make the membrane more rigid and reduce membrane fluidity

230
Q

Membrane content: protein content

A

Some membranes in the cell are very rich in protein and therefore have less movement in the membrane

231
Q

Parts of membrane protein

A

Signalling molecules
Intergins
Receptors
Channels and transporters
Anchors and junctions

232
Q

Signalling molecules

A

Include proteins involved in cell communication

233
Q

Integrins

A

Are membrane bound proteins that facilitate cell adhesion and cytoskeleton movement

234
Q

Receptors

A

On the surface of cells can facilitate endo or exocytosis or be used in cell signalling

235
Q

Channels and transporters

A

Moving material across the membrane

236
Q

Anchors and junctions

A

These proteins help cells move and attach to other cells and extracellular matrix

237
Q

Two categories of membrane transport

A

Passive and active

238
Q

Passive transport

A

Is movement of molecules across a membrane down their concentration gradient which does not require energy. Ie, simple diffusion or facilitated diffusion

239
Q

Channel mediated transport

A

Form pores allowing water and small charged molecules such as ions to pass through the hydrophobic membrane. Act as gates that open and close

240
Q

Carrier proteins

A

Undergo a conformational change to allow their cargo to pass from one side of the membrane to the other

241
Q

Active transport

A

Requires energy to move molecules across the membrane against their concentration gradient. Ie pump protein ATP used

242
Q

Direct active transporter

A

Antiporter pump. The pump directly uses ATP to create NA and K gradients

243
Q

Indirect active transport

A

Na/glucose supporter. It uses Na to create a glucose gradient (ATP no required)

244
Q

Two biochemical reactions

A

Catabolism
Anabolism

245
Q

Catabolism

A

Is the breakdown of cellular macromolecules with respect to cellular energy. Releases stored energy

246
Q

Anabolism

A

Is the production of cellular macromolecules. Consume the ATP produced by catabolism as small molecules are built into macromolecules (requires energy)

247
Q

What is ATP

A

Adenosine triphosphate is the primary energy source for cellular processes composed of adenine molecule, a ribose sugar and chain of three phosphates

248
Q

What is ADP

A

Adenosine diphosphate, when the third phosphate is removed from ATP

249
Q

What is GDP

A

Guanosine triphospahte identical to ATP except the adenosine is replaced with guanosine

250
Q

Other high energy molecules

A

NAD
fAD

251
Q

What is NAD

A

Nicotinamide adenine dinucleotide is converted to high energy form by the addition of an hydrogen ion and two electrons

252
Q

What is FAD

A

Is converted to high energy form by addition of two hydrogen ions and two electrons

253
Q

Cristae

A

Inner membrane appears to be closed in on itself to form structures

254
Q

Matrix

A

Inside the mitochondria is called the matrix this is where macromolecules are converted into small high energy compounds

255
Q

Three primary sources of energy

A

Carbs
Fats
Proteins

256
Q

Carbs

A

Stored as mainly glycogen in muscles and the liver. Muscle glycogen is more readily available for actively working muscle

257
Q

Fats

A

Stored as tricyglycerols throughout the body they must be broken down to release free fatty acids that need transported into the cells that need energy

258
Q

Proteins

A

Are stored in skeletal muscle which is why there is muscle wasting if the body needs to use proteins as an energy source

259
Q

Carbs three major classes

A

Monosaccharides
Disaccharide
Polysaccharide

260
Q

Monosaccharides

A

One sugar are most commonly consumed in the form of glucose

261
Q

Disaccharide

A

More complex consist of two mono bonded by alpha and beta glycosidic linkage

262
Q

Polysaccharide

A

Even more complex which are much longer chains of mono

263
Q

Brains main energy source

A

Glucose and ketones

264
Q

Heart main energy source

A

Fatty acids and some ketones

265
Q

Skeletal muscle main energy source

A

Glucose
Fatty acids
Ketones

Midterm PHGY 170 (1 decks)

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