Introduction to Microbial Groups and Biochemistry Review Videos

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41 Terms

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Parasitic worms, including tapeworms, roundworms, and flukes

Helminths

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Adult worms are usually large enough to see without a microscope, so they are

Not considered microorganisms

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Type: Bacterium

Typical location: Large intestine

Effects on health: Usually harmless and may help produce vitamin K. Certain strains cause diarrhea. Entering other body sites can cause UTIs or other infections.

E. coli

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Type: Fungus: usually a yeast

Typical location: Mouth, digestive tract, vagina, and skin

Effects on health: Usually lives harmlessly in small amounts. Overgrowth can cause thrush, vaginal yeast infections, skin infections, or bloodstream infections.

Candida albicans

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Type: Fungus, a mold

Typical location: Soil, decaying plants, dust, and air

Effects on health: Helps break down dead material. Inhaled spores can cause allergic reactions or lung infections, especially in people with weakened immunity.

Aspergillus species

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They kill microbes or stop their growth by targeting structures or processes such as cell walls, membranes, protein production, or DNA replication.

Antimicrobial medications

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What causes disease?

Pathogens

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What normally live on or inside the body without causing disease, although some can cause infection under certain conditions?

Resident microbiota

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What are some roles of resident microbiota in the body

Food digestion, vitamin production, immune system development, and prevent other microbes from taking over

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Greater exposure to blank may increase the chance of infection

Microbes

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A microbe’s ability to attach, invade, produce toxins, or escape immune defenses affects how much harm it causes

Virulence

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Factors that influence whether disease occurs

Number of microbes, Virulence, Location, Host defenses, Host health, and Microbiota balance

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Three important safety considerations in medical settings

Clean hands, Use appropriate protection, and Prevent contamination

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Resists changes in pH by accepting or releasing hydrogen ions (H⁺)

Buffer

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Releases H⁺. Has a pH below 7

Acid

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Accepts H⁺ or releases hydroxide ions (OH⁻). Has a pH above 7

Base

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Has a pH of 7, like pure water.

Neutral

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Each step on the pH scale represents a blank in H⁺ concentration

10-fold change

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Description: Sugars and chains of sugars

Subunits: Monosaccharides, such as glucose

Carbohydrates

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A distinct molecule, protein chain, or component that combines with other similar or different parts to form a larger, more complex functional structure

Subunits

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Description: Fats and other mostly water-insoluble molecules

Subunits: Many contain glycerol and fatty acids. Do not have one universal monomer

Lipids

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Description: DNA and RNA

Subunits: Nucleotides

Nucleic acids

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Description: Folded chains of amino acids

Subunits: Amino acids

Proteins

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  • Provide quick energy, especially glucose.

  • Store energy as glycogen in animals or starch in plants.

  • Provide structural support, such as cellulose in plant cell walls.

  • Help cells recognize and communicate with each other


Carbohydrates

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Store energy long term, insulate the body, and cushion organs. Each contains glycerol and three fatty acids

Triglycerides

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Form the cell membrane’s bilayer. Their heads attract water, while their tails repel water

Phospholipids

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Include cholesterol, which helps regulate membrane fluidity, and certain hormones

Steroids

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Provide protective, water-resistant coatings

Waxes

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Each nucleotide contains?

  • A phosphate group

  • A five-carbon sugar

  • A nitrogenous base


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What is the five-carbon sugar in DNA?

Deoxyribose

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What is the five-carbon sugar in RNA?

Ribose

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The five nitrogenous bases are?

adenine, guanine, cytosine, thymine, and uracil

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What are the DNA bases?

Adenine, thymine, cytosine, guanine

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What are the RNA bases?

Adenine, uracil, cytosine, guanine

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Act as enzymes, provide structural support, transport substances, allow movement, send signals, and defend against infection.

Proteins

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The covalent bond that joins two amino acids

peptide bond

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The order of amino acids in a chain

Primary

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Local folding into alpha helices or beta sheets, held by hydrogen bonds

Secondary

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The overall three-dimensional shape of one amino acid chain

Tertiary

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Two or more amino acid chains joining to form a functional protein

Quaternary

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The loss of a protein’s normal shape, often caused by heat, extreme pH, or chemicals. It usually causes loss of function without breaking the peptide bonds

Denaturation