Chapter 5 Flashcards

(40 cards)

1
Q

What are 6 carbon sugars called

A

Hexose

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2
Q

What are 5 carbon sugars called

A

Pentose

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3
Q

What are 3 carbon sugars called

A

Triose

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4
Q

Definition of saturated fats

A

Fatty acid that only has single bonds allowing more hydrogen atoms on the carbon skeleton

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5
Q

Definition of unsaturated fats

A

Fatty acids that have one or more double bond

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6
Q

What is trans fat

A

Unsaturated fat formed by hydrogenation of oils containing one or more trans double bonds

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7
Q

Definition of cholesterol

A

Steroid that forms part of cell membrane and act as a precursor for synthesis of other steroids

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8
Q

Functions of proteins

A

Catalyst, defense, storage, transport, communication, movement, structural support.

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9
Q

Catalyst term

A

Chemical agent that increases rate of a reaction without being consumed by it

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10
Q

Polypeptides

A

Polymer of many amino acids linked by peptide bonds

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11
Q

Protien

A

Biologically functional molecules consisting of 1 or more polypeptide with a specific formation

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12
Q

Amino acids

A

Organic molecule that has carboxyl and amino groups; monomer of polypeptide

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13
Q

What is the alpha carbon

A

The asymmetrical carbon in an amino acid

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14
Q

What is the r group

A

Distinguishing feature of amino acids

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15
Q

Primary structure

A

Linear, dictates secondary structure and tertiary structure

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16
Q

Secondary structure definition

A

Coiled or folded from hydrogen bonds, between the polypeptide backbone

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17
Q

What causes hydrogen bonding in secondary structures

A

The oxygen atoms negative charge and nitrogen atoms being slightly positive

18
Q

What causes alpha helix in secondary structure

A

Coil held together by hydrogen bond between every 4th amino acid

19
Q

what is the Beta pleated sheet

A

The folds in secondary structure, 2 or more segments of polypeptide lying parallel connected by hydrogen bonds

20
Q

What is tertiary structure

A

Overall 3D shape resulting from polypeptides interacting with side chains

21
Q

What is a hydrophobic interaction in amino acids

A

Type of interaction in amino acids with non polar R groups that end up in clusters at its core

22
Q

In tertiary structures what holds nonpolar bonds

A

Van deer walls interaction

23
Q

What bonds holds the tertiary structure together

A

hydrogen bonds (between polar R groups) and ionic bonds (between positive and negative R groups)

24
Q

What bonds reinforces the shape of tertiary structures

A

Disulfide bridges or covalent bonds

25
What is quaternary structure
contain 2 or more polypeptides chains combined into one functional protein
26
Biology perspective of sickle cell disease
Disease caused by nucleotide change in alpha globin gene causes hemoglobin to aggregate changing cell shape
27
Denaturation definition
For proteins, a process which disruption of weak chemical bonds and interactions make proteins lose their innate shape
28
What technique is used to study 3-D shape of molecules
X-ray crystallography
29
What is nucleic acid
Polymer of nucleotides
30
Function of RNA
Protein synthesis, gene regulation, and genome for viruses
31
What is the flow of genetic information
DNA>RNA>protein
32
What synthesis mRNA
DNA
33
Function of mRNA
Interact with ribosomes to direct production of polypeptides
34
Where is DNA located
Nucleus
35
Where does mRNA relay information
Cytoplasm
36
What is a nucleoside
Portion of nucleotide without a phosphate group; lost after polymerization
37
What are nitrogenous bases
Have 1-2 rings that include nitrogen atom. They are bases because the nitrogen tends to be basic in solutions
38
What is pyrimidines
One six membered ring
39
Purines
One six membered ring fused to a five membered ring
40
What bond forms sugar phosphate backbone of nucleic acid
Phosphodiester bond