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Biology Of Cells > Biology of Cells > Flashcards

Biology of Cells Flashcards

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AP® Biology flashcards Biology 101 flashcards
0
Q

Bacteria

A

One of two prokaryotic domains

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1
Q

Archaea

A

One of two prokaryotic domains, lives in extremes (high/low PH, heat etc)

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2
Q

Domain

A

Taxonomic category, above the kingdom level. Includes eukaryotic and prokaryotic (archaea, bacteria) cells

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3
Q

Eukarya

A

Domain that includes all eukaryotic organisms - Animalia, fungi, plantae, protists

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4
Q

Eukaryotic

A

Type of cell with a membrane-enclosed nucleus and membrane-enclosed organelles.

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5
Q

Prokaryotic

A

Type of cell lacking a membrane-enclosed nucleus and membrane-enclosed organelles

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6
Q

Cell Theory

A
  • All living organisms are composed of cells. They may be unicellular or multicellular.
  • The cell is the basic unit of life.
  • Cells arise from pre-existing cells.
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7
Q

Types of microscopy

A

Light Microscopy

  • Bright field: stained and unstained, most common type of microscopy. Limit 0.2 micro meters
  • Confocal: shows a 3D image,
  • Fluorescent: uses ultra violet light instead of light to bring out different colours of the dye that stains the specimen 0.17 micro meter resolution limit (due to shorter wave length of UV light

Electron Microscopy (2nm/0.002micro metres)

  • Transmission Electron Microscope (TEM): 2D image through a thin slice of specimen.
  • Scanning Electron Microscope (SEM): 3D scanned image of the surface of a specimen, less magnification but greater depth
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8
Q

Deductive reasoning

A

An analysis of data gained by observation and description can lead to conclusion

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9
Q

Inductive reasoning

A

Seeks to explain nature through observation, questioning, making hypothesis, running tests and making conclusions (scientific method)

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10
Q

Hypotheses

A

Suggestions put forward as possible explanations of observations

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11
Q

Prediction

A

If Hypothesis is correct you are predicting something to happen under certain conditions

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12
Q

Nucleotide

A

Bases of DNA (rungs of the double helix ladder)

Adenine pairs with thymine (uracil in RNA)

Guanine pairs with cytosine

Pyrimdians- cytosine, thymine, uracil. Six sided ring

Purines- adenine, guanine. Six sided attached to five sided ring.

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13
Q

DNA

A

Nucleic acid macromolecule, double strand helix, each polynucleotide strand consists of nucleotide monomers with a deoxyribose sugar. Capable of being replicated and determining the inherited structure of a cells protein.
Strands of DNA form in an antiparallel configuration where (top and tail) where one strand starts with the pentose the 5 prime carbon, the other will start with the 3 prime carbon

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14
Q

Building block principle

A

All macromolecules are made with the same sort of process.

Building blocks are monomers that form together through hydrolosis and dehydration reactions using energy and enzymes.

Each end of a polymer is always different

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15
Q

Macromolecules

A

Nucleic acid, protein, polysaccharides (all polynucleotide polymers) and lipids

Nucleic acids (DNA/RNA)made of adenine, thymine, guanine, cytosine and uracil (monomers) coding for proteins. (C,H,O,P,N)

Proteins - made of 20 amino acids (monomers) peptide bonds to form complex polypeptides (C,H,O,N(S)(P))

Polysaccharides - carbohydrates, polymers are Starch, cellulose, glycogen and chitin. All made of simple sugar (monosaccharides, disaccharides, olisaccarides) (C,H,O)

Lipids - include fats, phospholipids and steroids
Made of glycerol and fatty acids. Bonded by ester linkage (C,H,O (P)(N))

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16
Q

Bonds

A

Covalent bond: two atoms share one or more valence electrons

Ionic bond: atoms lose or gain electrons to complete their valence electron layer

Hydrogen bond: weak chemical bond between the slightly positive hydrogen atom in a polar covalent bond is attracted to a slightly negative hydrogen ion in a polar bond in another part of the same molecule.

Van der waals interactions: weak attractions between molecules or parts of molecules that result from transient local partial charge.

Hydrophobic interactions: molecules that do not mix with water join to exclude water

17
Q

Nucleoside

A

Nucleotide (A,G,T,C,U) plus a five carbon sugar (pentose)

18
Q

Active site

A

Part of an enzyme that binds the substrate and that forms the pocket in which catalysis occurs

19
Q

Amino acid

A

Organic molecule consisting of a carboxylate group (C,O) and amino (N,H) makes proteins

20
Q

Conformation

A

The shape/form a protein takes is decided by all the amino acids at the primary structure and how they fold/interact. The polar and non polar aminos all fold and interact together. The polypeptide then folds in a way based on these bonds to protect the hydrophobic side r groups from water. Conformation of protein is designed to be ideal for the current environment e.g water. If that environment changes (heat,ph,salinity) then the polypeptide denatures (sometimes beyond repair)

21
Q

Protein layers

A

Primary: sequence of amino acids

Secondary: hydrogen bonds between aminos (excluding side chains) pleated sheet or helix shape

Tertiary: interactions (VDW, H, CV bonds) between side chains. Forms overall structure.

Quaternary: how multiple polypeptides intertwine

22
Q

Enzyme/substrate

A

Enzymes are proteins that are used to speed up reactions without being consumed by the reaction. Every enzyme works with a specific substrate eg sucrase works with sucrose.

23
Q

Amphipathic

A

Having both a hydrophobic and a hydrophilic region

E.g phospholipids

24
Q

Cell membrane

A

Double Phospholipid layer with hydrophobic regions joined,

25
Q

Diffusion

A

Movement of particles from high to low concentration areas

26
Q

Endocytosis/exocytosis

A

Endocytosis - cellular uptake of biological molecules, via formation of vesicles from plasma membrane.

Exocytosis - cellular secretion of biological molecules by fusion of vesicles containing them with the plasma membrane

27
Q

Fat

A

Made up of three fatty acid chains attached to a glycerol molecule

Saturated fat - no double bond in the carbon chain of fatty acids, leading to a saturation of hydrogen molecules

Unsaturated fat - has at least one double bonded carbon, either cis kink (natural) or trans kink (artificially made)

28
Q

Fluid mosaic model

A

Cell membrane structure - mosaic of protein molecules drifting laterally in a bilayer of phospholipids

29
Q

Glycolipid

A

A lipid with one or more covalently attached carbohydrate

30
Q

Glycolipid

A

Protein with one or more carbohydrate covalently attached

31
Q

Integral protein

A

Protein that sits amongst phospholipid bilayer of cell membrane, hydrophilic region extend out each side of phospholipids while hydrophobic region remains in between phospholipids

32
Q

Peripheral protein

A

A protein on the outside of a cell membrane often attached to the cell membrane or an integral protein. Not embedded in the phospholipid bilayer

33
Q

Rough endoplasmic reticulum

A

Responsible for protein synthesis - secreted and membrane proteins

Glycosylation- formation of glycoproteins (sugar + protein)

Membrane synthesis

Roughness is ribosomes, free space between folds is called lumen

34
Q

Smooth endoplasmic reticulum

A

Ca2+ storage (eg muscle contraction)

Lipid synthesis (e.g steroid sex hormones)

Poised detoxification (e.g alcohol)

35
Q

Ribosomes

A

Made up of small and large subunit

Is the site of protein synthesis - mRNA brings amino acids to ribosome and the ribosome forms a protein

Protein will either travel to a cellular organelle or enter the rough ER to be secreted from the cell

36
Q

Journey of proteins in the cell including Exocytosis

A

Process where ribosomes synthesise a polypeptide destined to become a protein for the cell membrane or beyond, a signal peptide is attached to the polypeptide to guide it to a signal recognition particle (SRP), the SRP latches onto a signal receptor on the rough ER, the SRP leaves, the protein enters the rough ER leaving the signal peptide behind, the ribosome leaves and splits into pieces (small, large subunits plus mRNA), the polypeptide inside the rough endoplasmic reticulum synthesises into a fully formed protein, glycosylation can also take place in the rough ER where a sugar molecule is covalently bonded to the protein (helps protein folding and stops quick destabilisation). The protein/glycoprotein leaves the rough ER in a broken off piece of rough ER called a vesicle, the protein/glycoprotein is transported to the Golgi apparatus where the vesicle fuses into the receiving face and membrane flows forward moving the proteins towards the shipping face, glycoproteins are developing by fusing with sugars during this period, (exocytosis begins) the proteins/glycoproteins are then broken off into vesicles and fuse with the cell wall, proteins are released into the extra cellular space while the sugary glycoproteins stay attached to the vesicle which is now a part of the cell wall facing the extra cellular space.

37
Q

Vacuoles

A

Used for ion/organic compound storage

Some have hydrolytic enzymes (enzymes that use water to break down substrates)

Derived from ER and Golgi

38
Q

Lysosomes

A

Sometimes when proteins/glycoproteins exit the Golgi in a vesicle, instead of fusing to the cell membrane and releasing proteins, a lysosomes is created

  • causes phagocytosis (breaks down food brought into cell)
  • autophagy - digests old organelles
  • autolysis - destroys cells in development
39
Q

Endomembrane system

A

Manufacturers, sorts and distributes
Physical continuity
Transfer of vesicles

  • endoplasmic reticulums
  • nuclear envelope
  • Golgi apparatus
  • plasma membrane
  • lysosomes
  • vacuoles (in plants and fungi)
40
Q

Chromatin

A

Complex of macromolecule cells - DNA, RNA and protein

Inside nucleus

Biology Of Cells (1 decks)

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