AP Anatomy and Physiology

AP Anatomy and Physiology

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Section 1

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Solvency

Front

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Cards (66)

Section 1

(50 cards)

Solvency

Front

Water is often called the Universal Solent for its ability to dissolve a wide variety of substances.

Back

Saturated

Front

No carbon-carbon double bonds.

Back

Hydrogen Bonding

Front

The properties of water are primarily due to its polarity. The electrons in the O-H bond are not shared equally. This results in a partial negative charge on the oxygen and a partial positive charge on the hydrogen.

Back

CHNOPS

Front

The elements essential for life. Carbon, hydrogen, nitrogen, oxygen, phosphate, sulfur

Back

Glycogen

Front

A highly branched chain of glucose molecules. Found in animals to store energy.

Back

Amino acids

Front

There are 20 different amino acids. All amino acids contain one amino group, a carboxyl group, and one variable(R-group). The R-groups which determines the properties of each amino acid

Back

Methyl

Front

R-CH3 Non-polar. Found in fatty acids.

Back

Phosphate

Front

O " R-P-OH | OH Polar. Found in nucleotides and phospholipids.

Back

Buffers

Front

Substances which resist changes in pH. They are often weak acids and bases. Bicarbonate is a common buffer in blood which is kept at ~7.4

Back

Organic Molecules

Front

An organic molecule contains carbon and hydrogen.

Back

Lipids

Front

Fats and oils(triglycerides) Waxes Steroids Phospholipids

Back

Sulfhydryl

Front

R-SH Forms disulfide bond. Found in some amino acids.

Back

Thermal Stability

Front

Water requires more heat energy to raise its temperature. It resists change in temperature.

Back

Peptide

Front

Contains few amino acids and a polypeptide(protein) contains many

Back

Proteins

Front

Structural: (Ex: keratin, silk) Enzymes: (Ex: catalase, trypsin) Transport: (Ex: hemoglobin, potassium channel) Defense: (Ex: antibodies) Hormones: (Ex: Insulin) Motion: (Ex: myosin) Storage: (Ex: ferritin, casein) Receptor: (Ex: insulin receptor)

Back

Chitin

Front

The structural carbohydrate of fungi and animals. Found in the exoskeleton of crabs and insects.

Back

Hydrophilic

Front

'Water-loving' and will readily dissolve in water. They have polar functional groups.

Back

Polymer

Front

Molecules made up of large numbers of repeating monomers. Organic macromolecular polymer can contain between 2 and billions of monomers.

Back

Steroids

Front

Function: Hormones and membrane stabilizer No true monomer exists. Steroids consist of several carbon rings. Elements: CHO All steroids are highly hydrophobic.

Back

Disaccharides

Front

Glucose + Glucose = Maltose Glucose + Galactose = Lactose Glucose + Fructose = Sucrose

Back

Hexoses

Front

6 carbon sugars Glucose, Galactose, and Fructose

Back

Adhesion/Cohesion

Front

Water 'sticks' to substances. This allows it to act as a lubricant in our body. It also has a high surface tension.

Back

Isomer

Front

Organic molecules which have the same molecular formula but have a different arrangement of atoms. This can result in the isomers having different functional groups.

Back

Fats and oils (triglycerides)

Front

Function: Long-term energy and insulation Each triglyceride is made up of a molecule of a glycerol and three fatty acids Lipids containing saturated fatty acids are fats. Those with unsaturated fatty acids are oils. Elements: CHO All triglycerides are highly hydrophobic.

Back

Hydroxyl

Front

R-OH Polar. Forms hydrogen bonds. Found in sugars and some amino acids.

Back

Hydrolysis

Front

This reaction breaks down a polymer into monomers. A molecule of water is used in the process.

Back

Density

Front

Liquid water is more dense than ice.

Back

Water

Front

Properties Essential for Life: 1) Solvency 2) Adhesion/Cohesion 3) Density 4) Thermal Stability

Back

Monosaccharides

Front

Used for energy and they consist of carbon rings. Hexoses Pentoses

Back

Starch

Front

A chain of glucose molecules found in plants to store energy.

Back

Protein continued

Front

Monomers: amino acids, the bond between amino acids is called a peptide bond Polymer: peptide, proteins can have up to 4 levels of structure Conditions which affect hydrogen bonding, or hydrophilic/hydrophobic interactions, alter the shape of the protein or its folding. These include temperature, pH, pressure, and salinity(salt)

Back

Pentoses

Front

5 carbon sugars Ribose and Xylose

Back

Carboxyl

Front

O " R-C-OH Polar. Acidic. Found in fatty acids and amino acids.

Back

pH

Front

Defined as the -log[H+]

Back

Unsaturated

Front

Has carbon-carbon double bonds.

Back

Protein continued 2

Front

Proteins which have lost their shape or unfold are said to be denatured The 3D shape of a protein is critical to its function Elements: CHONS Depending on their variable group(R-group), amino acids can be either hydrophilic or hydrophobic. Often the protein as a whole has large sections that are one or the other

Back

Polysaccharides

Front

Used for energy storage and structure. Due to their size and bonding structure, they tend to be insoluble.

Back

Cellose

Front

Structural carbohydrate of plants. It is found in cell walls.

Back

Carbonyl

Front

O " R-C-H Polar. Found in sugars.

Back

Dehydration Reaction

Front

This reaction joins two monomers together to form a polymer. In this process a molecule of water is released.

Back

Functional Groups

Front

The reactivity of organic molecules depends upon its functional group. 1) hydroxyl 2) methyl 3) carbonyl 4)carboxyl 5) amino 6) phosphate 7) sulfhydryl

Back

Waxes

Front

Function: Water-proofing Made up of s long-chain alcohol and a fatty acid. Elements: CHO All waxes are highly hydrophobic.

Back

Enzyme

Front

An enzyme is a biological catalyst

Back

Amino

Front

R-NH2 polar. Forms hydrogen bonds. Found in amino acids. Basic.

Back

Bases

Front

Substances which except protons. Has a pH between greater than 7 and 14.

Back

Carbohydrates

Front

Primarily immediate energy but they are also structural. Monomers: monosaccharides Polymers: disaccharides and polysaccharides Elements: monomers have the general formula of CnH2nOn n = the number of carbons Carbohydrates are highly hydrophilic

Back

Phospholipids

Front

Function: Main component of cell membrane Consist of a glycerol attached to two fatty acids and a phosphate group. Elements: CHOP Phospholipids are amphilic. The phosphate groups is hydrophilic and the rest of the molecule is hydrophobic.

Back

Hydrophobic

Front

'Water-fearing' and will not readily dissolve in water. They have non-polar functional groups.

Back

Catalyst

Front

Something that speeds up a reaction but does not change in the process

Back

Acids

Front

Substances which donates protons. Has a pH between 0 and less than 7.

Back

Section 2

(16 cards)

Tertiary

Front

Charged/polar properties of proportions of the protein(R-group) forces it to fold into its 3D globular shape

Back

Nucleic acids

Front

The genetic material of the cell. Nucleotides are often parts of coenzymes, like ATP, which are critical to the function of the cell Monomer: nucleotides Polymer: deoxyribonucleic acid(DNA) and ribonucleic acid(RNA) Elements: CHONP Nucleic acids are hydrophilic

Back

Pyrimidines

Front

cytosine(C), thymine(T), uracil(U)

Back

Denatured

Front

Proteins which have lost their shape or unfold

Back

Quaternary

Front

Multiple proteins come together to form this level of structure. It is held together by hydrogen bonds and R-group interactions between subunits

Back

Primary

Front

Determined by the amino acid sequence

Back

rRNA

Front

Ribosomal RNA. It catalyzes peptide bond formations

Back

ribonucleic acid (RNA)

Front

Three types: mRNA, tRNA, and rRNA Four nucleotides: adenine, cytosine, guanine, and uracil Always single-stranded. However, it can fold back on itself and form a 3D structure Found throughout the structure

Back

Nucleotides

Front

Each nucleotide is made up of three parts: phosphate, sugar, and nitrogen base There are two types of nucleotides: purines and pyrimidines. A purine can form hydrogen bonds with a pyrimidine( A-T/U, C-G)

Back

Purines

Front

Adenine (A) and Guanine (G)

Back

Prions

Front

Misfolded proteins which cause disease by getting other proteins to fold incorrectly Ex: Mad Cow Disease and Creutzfeldt-Jakob Disease

Back

tRNA

Front

transfer RNA. It brings amino acids to the ribosome

Back

deoxyribonucleic acid (DNA)

Front

Four nucleotides: adenine, cytosine, guanine, and thymine DNA consist of two strands bonded by hydrogen bonds Found only in the nucleus

Back

Chaperones

Front

Proteins which help other proteins fold correctly

Back

mRNA

Front

messenger RNA. It acts as a working copy which leaves the nucleus and binds the ribosome

Back

Secondary

Front

Held together by hydrogen bonds between amino acids cause portions of the protein to fold to form an Alpha Helix or a Beta Sheet

Back