03 - Biomolecules Flashcards

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1
Q

Halocarbons

A

Single bonds , double carbon-carbon bonds

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2
Q

Double lines

A

Double bonded

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3
Q

Hydroxyl group?

A

(OH) , polar

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4
Q

Carbonyl group?

A

Carbon double bonded to oxygen, polar

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5
Q

Ketone?

A

Carbonyl group within skeleton, in the middle.

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6
Q

Aldehyde?

A

Carbonyl group at the end, slanted.

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7
Q

Carboxyl group?

A

(–COOH) , very polar and acidic (donates H+)

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8
Q

Amino group?

A

(–NH2), very polar and basic (picks up H+)

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9
Q

Sulfhydryl group

A

(–SH) or (–HS), polar, cross link in proteins

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10
Q

Phosphate group

A

(–OPO3^2-), Very polar and negatively charged

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11
Q

Methyl Group

A

(–CH3), Nonpolar

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12
Q

Dehydration reaction

A

A dehydration reaction in biology is a type of chemical reaction where two molecules combine to form a larger molecule, accompanied by the loss of a water molecule (H₂O)

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13
Q

Hydrolysis reaction

A

A hydrolysis reaction in biology is a chemical process in which a molecule is broken down into smaller units by the addition of a water molecule (H₂O)

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14
Q

three important biomolecules that are polymers:

A

carbohydrates, proteins, and nucleic acids

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15
Q

Glycosidic dehydration reaction

A

A glycosidic dehydration reaction is a specific type of dehydration reaction in which two monosaccharides (simple sugars) are joined together to form a disaccharide (or a larger carbohydrate, polysaccharide) through the formation of a glycosidic bond, accompanied by the loss of a water molecule (H₂O).

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16
Q

Ester dehydration reaction

A

a bond between a hydroxyl group and a carboxyl group

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17
Q

Carbohydrates

A

include sugars and polymers of sugar

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18
Q

Monosaccharides

A

(from the Greek monos, single, and sacchar, sugar) generally have molecular formulas that are some multiple of the unit CH2O, glucose is most common monosaccharide

19
Q

Polysaccharides

A

are macromolecules, polymers with a few hundred to a few thousand monosaccharides joined by glycosidic linkages

20
Q

Glucose

A

Sugar (C6H12O6)

21
Q

Lipids

A

are grouped with each other because they share one important trait: They are hydrophobic

22
Q

Triglycerides

A

fat molecules, The completed fat consists of three fatty acids linked to one glycerol molecule. (Other names for a fat are triacylglycerol and triglyceride

23
Q

Fatty acids

A

A carboxylic acid with a long carbon chain

24
Q

Steriods

A

are lipids characterized by a carbon skeleton consisting of four fused rings

25
Q

Cholesterol

A

a type of steroid, is a crucial molecule in animals

26
Q

Protein

A

A biologically functional molecule consisting of one or more polypeptides folded and coiled into a specific three-dimensional structure.

27
Q

Amino acids

A

is an organic molecule with both an amino group and a carboxyl group

28
Q

Polypeptide

A

A polymer of many amino acids linked together by peptide bonds.

29
Q

R groups

A

a side chain specific to each amino acid that confers particular chemical properties to that amino acid

30
Q

Amino groups

A

A chemical group consisting of a nitrogen atom bonded to two hydrogen atoms; can act as a base in solution, accepting a hydrogen ion and acquiring a charge of 1+.

31
Q

Nonpolar amino acids

A

a group of amino acids that are hydrophobic, meaning they do not mix well with water.

32
Q

Polar amino acids

A

amino acids with side chains that contain electronegative atoms, such as oxygen or nitrogen, that make them hydrophilic, or water-loving

33
Q

Polar and ionic amino acids

A

either acidic or negatively charged b/c they donated proton to water, or basic- accepted a proton

34
Q

Peptide bond

A

The covalent bond between the carboxyl group on one amino acid and the amino group on another, formed by a dehydration reaction.

35
Q

Primary structure

A

The level of protein structure referring to the specific linear sequence of amino acids.

36
Q

Secondary structure

A

Regions of repetitive coiling or folding of the polypeptide backbone of a protein due to hydrogen bonding between constituents of the backbone (not the sidechains).

37
Q

Tertiary structure

A

The overall shape of a protein molecule due to interactions of amino acid side chains, including hydrophobic interactions, ionic bonds, hydrogen bonds, and disulfide bridges

38
Q

Quaternary structure

A

The particular shape of a complex, aggregate protein, defined by the characteristic three- dimensional arrangement of its constituent subunits, each a polypeptide.

39
Q

Disulfide bridges

A

A strong covalent bond formed when the sulfur of one cysteine monomer bonds to the sulfur of another cysteine monomer.

40
Q

Nucleic acids

A

A polymer (poly-nucleotide) consisting of many nucleotide monomers; serves as a blueprint for proteins and, through the actions of proteins, for all cellular activities. The two types are DNA and RNA.

41
Q

Nucleotide

A

The building block of a nucleic acid, consisting of a five-carbon sugar covalently bonded to a nitrogenous base and one to three phosphate groups.

42
Q

Pyrimidine

A

One of two types of nitrogenous bases found in nucleotides, characterized by a six-membered ring. Cytosine (C), thymine (T), and uracil (U) are pyrimidines.

43
Q

Purine

A

One of two types of nitrogenous bases found in nucleotides, characterized by a six-membered ring fused to a five-membered ring. Adenine (A) and guanine(G) are purines.

44
Q

Phosphodiester bond

A

a chemical bond that connects nucleotides in a nucleic acid chain