Chapter 5 Flashcards

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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
Q

What is quaternary structure

A

contain 2 or more polypeptides chains combined into one functional protein

26
Q

Biology perspective of sickle cell disease

A

Disease caused by nucleotide change in alpha globin gene causes hemoglobin to aggregate changing cell shape

27
Q

Denaturation definition

A

For proteins, a process which disruption of weak chemical bonds and interactions make proteins lose their innate shape

28
Q

What technique is used to study 3-D shape of molecules

A

X-ray crystallography

29
Q

What is nucleic acid

A

Polymer of nucleotides

30
Q

Function of RNA

A

Protein synthesis, gene regulation, and genome for viruses

31
Q

What is the flow of genetic information

A

DNA>RNA>protein

32
Q

What synthesis mRNA

A

DNA

33
Q

Function of mRNA

A

Interact with ribosomes to direct production of polypeptides

34
Q

Where is DNA located

A

Nucleus

35
Q

Where does mRNA relay information

A

Cytoplasm

36
Q

What is a nucleoside

A

Portion of nucleotide without a phosphate group; lost after polymerization

37
Q

What are nitrogenous bases

A

Have 1-2 rings that include nitrogen atom. They are bases because the nitrogen tends to be basic in solutions

38
Q

What is pyrimidines

A

One six membered ring

39
Q

Purines

A

One six membered ring fused to a five membered ring

40
Q

What bond forms sugar phosphate backbone of nucleic acid

A

Phosphodiester bond