Lecture 3 (Chemical components of Cell) Flashcards

1
Q

Covalent bonds are when:

A

Atoms fill their outer shell by sharing electron pairs

Sometimes, one atom will attract an electron pair better than its partner (Polar molecules)

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2
Q

What are the 3 non covalent bonds?

A

Ionic, Hydrogen and Van der Waals

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3
Q

Ionic bonds are when:

A

A positive and negative atom attract to one another (+ and -)

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4
Q

Hydrogen bonds are when

A

an electropositive hydrogen attracts to an electronegative atom (polar atoms)

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5
Q

Water is important because:

A

Water can form weak
interactions with many polar
organic molecules like amino
acids and sugars.

▪ Water helps maintain the
structure and function of
macromolecules and the
complexes that they form.

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6
Q

What is an Acid, Base, Amphoteric, and Buffers?

A

▪ Acids release protons.
▪ Bases accept protons.
▪ Amphoteric molecules can act as either acids or bases.
▪ Buffers in living systems resist changes in pH

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7
Q

what are the 4 types of Macromolecules?

A

proteins,
nucleic acids,
polysaccharides, and
certain lipids

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8
Q

What are lipids? What types of Lipids are there?

A

Lipids dissolve in organic
solvents, not water.

▪ Important cellular lipids include
fats, steroids, and phospholipids.

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9
Q

What is the primary function of Carbohydrates?
Why does it dissolve in water?

A

stores of chemical
energy and as materials for biological construction.

highly water soluble due to their hydroxyl groups.

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10
Q

What are proteins? what are they made of?

A

macromolecules that carry
out a cell’s activities.

made of amino acid
monomers.

▪ Twenty different amino acids,
with different chemical
properties, are commonly used
in the construction of proteins.

▪ All amino acids have a carboxyl
and an amino group, separated
by a single carbon atom

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11
Q

What is the Primary structure of Protein?

A

the amino acid sequence of a protein

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12
Q

What is the Secondary Structure of proteins?

A

the conformation of portions of the
polypeptide chain depending on the amino acid
sequence

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13
Q

What is the tertiary structure of Proteins?

A

describes the conformation of the entire polypeptide.

are categorized by shape as either fibrous
proteins, which are elongated, or globular proteins, which are compact.

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14
Q

What is the Quaternary Structure of proteins?

A

Proteins composed of subunits linked by
covalent disulfide bonds or held together by noncovalent bonds are said to have quaternary
structure.

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15
Q

What is denaturation of a protein?

A

The unfolding of a protein

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16
Q

What is a molecular chaperon’s function and where do they bind?

A

molecular chaperones, bind to short stretches of
hydrophobic amino acids to help unfolded proteins achieve their proper
3D conformation.

17
Q

What is a proteomic?

A

The entire inventory of proteins that is produced by an organism

18
Q

What are nucleic acids?

A

polymers of nucleotides that store and
transmit genetic information.

19
Q

What are nucleotides made of?

A

nucleotide consists of three parts:
a five-carbon sugar,
a phosphate group,
and a nitrogenous base

20
Q

What are the pairings of nitrogenous bases that exist in DNA and RNA?

A

Both: Purines of Adenine and Guanine
DNA only: the pyrimidines Thymine and Cytosine
RNA Only: The pyrimidines Uracil and Cytosine

21
Q

What are ribozymes?

A

RNA enzymes with catalytic activity

22
Q

Describe the roles of electrons in the formation of
covalent bonds.
▪ Describe the role of noncovalent bonds in the structure
of molecules such as water.
▪ Explain the characteristics of acids, bases, and buffers.
▪ Describe the general structure and functions of biological
molecules.
▪ Identify the monomers, the synthesis and the functions
in the cell of the four types of biological molecules.

A