Module 1 Flashcards

(32 cards)

1
Q

What is molecular biology

A

Study of essential cellular macromolecules, including DNA, RNA and proteins

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2
Q

What is the central dogma?

A

DNA -> RNA -> Protein,

DNA to RNA is done by transcription,
RNA to DNA is reverse transcription
RNA to protein is done by translation
DNA back to DNA is replication

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3
Q

What is a chemical bond?

A

atoms that are held together through chemical forces known as chemical bonds

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4
Q

Covalent bond

A

formed when 2 atoms share a pair of electrons between their positively charged nuclei

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5
Q

ionic bond

A

involves complete transfer of 1 electron to another (greater than 1.67 on the pauling scale)

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6
Q

electronegative

A

tendency to gain electrons

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7
Q

electropositive

A

tendency to lose electrons

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8
Q

Polar covalent

A

pauling scale is greater than 0 and less than 1.67, electrons are shared between atoms but biased towards 1 pole

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9
Q

What type of process is bonding?

A

exothermic

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10
Q

Van der waals interaction

A

depends heavily on the distance between interacting atoms

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11
Q

Hydrogen bond

A

attractive intermolecular forces between 2 partial element charges of opposite polarity. One partner in the bond must be a hydrogen which must be bonded to something strongly electromagnetive like such as oxygen, nitrogen, fluoride

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12
Q

Chiral

A

molecule with a structure that cannot be superimposed on its mirror image. all nucleic acids and proteins are chiral

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13
Q

stereoisomes

A

pairs of molecules that have some chemical and structural formulas but are not superimposable on 1 another

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14
Q

Enantiomers

A

pairs of stereoisomers that are mirror images of 1 another

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15
Q

scientific method parts

A
  • hypothesis and discovery
  • model building calculation
  • exploration and observation
  • inspiration
  • serendipity
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16
Q

What are the three components of a nucleotide

A

phosphate group, pentose sugar, nitrogenous base
(AGCT)

17
Q

Polypeptide

A

chain of amino acids, functional proteins can be composed of a single polypeptide or multiple peptide subunits

18
Q

What are the base pairs of DNA

19
Q

How are the nucleotides linked?

A

by phosphodiester bonds

20
Q

ribonucleotides

A

RNA nucleotides have 1 more hydroxyl group on the sugar ring than deoxyribose

21
Q

how are amino acids joined together

A

peptide bonds

22
Q

What is amino acid structure?

A

central carbon, bonds to amino group, carboxyl group, hydrogen and side chain

23
Q

what are the 4 group categories?

A
  • nonpolar aliphatic R groups
  • polar uncharged R groups
  • polar, charged R groups
  • nonpolar aromatic R groups
24
Q

Primary structure

A
  • sequence of amino acids, along with any disulfide linkages between cysteine residues
  • linked by peptide bonds
  • atoms of a peptide bond and the alpha carbons connected to them lie in L plane, due to partial double bond between carbonyl and amide groups, giving rise to cis and trans isomers- trans more common
25
Secondary structure
regularly repeating elements within a protein, in which hydrogen bonds form between polar atoms in the backbone chain main structures are alpha and beta helix
26
alpha helix
contains 3.6 amino acid residues per turn, internal hydrogen bonds set up electric dipole for entire helix. unfavorable for certain conditions of residuals beuase the confined geometry of the ring can distort helix
27
beta sheet:
formed by hydrogen bonding between 2 peptide segments in the beta conformation, eitherr within a polypeptide chain or separate polypeptide chains, can have parallel or antiparallel configurations
28
tertiary structure
3D structure consisting of structural elements or loops
29
protein doman
independent folding unit within a protein and consists of 150 residues
30
supersecondary element / structural motif
arrangement of multiple secondary structural elements typically found in proteins are the building blocks associated with particular functions
31
quaternary structure
includes all the connections between 2 or more polypeptides and can range from a simple homodiner to a large ribosome
32
categories of key protein functions
-structure facilitate protein folding: chaperones, chaperonins, protein isomerases