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Introduction to Biotech > Exam 1: Biomolecules and Enzyme Kinetics > Flashcards

Exam 1: Biomolecules and Enzyme Kinetics Flashcards

1
Q

Name the four macromolecules (biomolecules) within the cell and their building blocks:

A

Sugars (glycans), Fatty Acids (lipids), Amino Acids (proteins), Nucleotides (Nucleic Acids) FANS

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2
Q

Give examples of biomolecules

A

Fatty Acids: Fats
Amino Acids: Enzymes
Nucleotides: RNA, DNA
Sugar polysacchrides

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3
Q

Describe central dogma of biology

A

DNA creates RNA through transcription, RNA creates proteins through translation

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4
Q

About DNA (macro view)

A

Deoxyribonucleic Acid, instructions for creating proteins, inherited instructions, made of nucleotides

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5
Q

Components of nucleotides

A

5-carbon sugar (deoxy), phosphate, and nitrogenous base

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6
Q

How can you distinguish between rna and dna

A

Deoxyribose vs ribose sugar, DNA is missing an OH group on the second carbon of the ribose sugar (2-deoxyribo)

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7
Q

Categorize the nitrogenous bases which make up DNA

A

Purines: Adenine and Guanine
Pyrimidines: Cytosine, Uracil (RNA), Thymine (DNA)

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8
Q

About nucleoside and naming

A

Nucleosides= Nucleobase + sugar
if base is purine: ending is -osine
if base of pyridine: ending is -idine
if deoxy sugar, add deoxy-

ex: adenosine, deoxyadenosine, cytidine

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9
Q

Two types of nucleotides

A

ribonucleosides, and deoxyribonucleosides

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10
Q

Impossible nucleosides

A

Thymidine, Thymidine monophosphate, deoxyuridine, deoxyuridine monophosphate

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11
Q

Purpose of phosphate group in DNA

A

serves as linkers to form nucleic acids, provides polarity (5’ vs 3’) end, base sequences can vary, phosphodiester linkage

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12
Q

Alternate functions of nucleotides other than forming nucleic acids

A

carrying energy of hydrolyzes phosphoanhydride bonds (ATP), forming coenzymes, acting as signaling molecules

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13
Q

Forming dsDNA

A

hydrogen bonding holds two nucleotides together, two h-bonds between T/U-A and three between G/C (G/C is a stronger and shorter bond)

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14
Q

About dsDNA structure

A

two interconnected, right handed double helix structure, antiparallel strands

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15
Q

How many base pairs in the human genome?

A

3,000,000,000

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16
Q

How is the genome organized, start from DNA

A

DNA is organized intro strings of chromatin, which are wrapped around histones to form nucleosomes, these nucleosomes continue to bind into two chromatids held together by a centromere to form a chromosome

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17
Q

Name DNA replication enzymes

A

DNA helicase, RNA primase, DNA polymerase I, II, III, ss-binding proteins, DNA ligase, Sliding clamp, topoisomerase

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18
Q

DNA replication: purpose of DNA helicase

A

unwinds DNA double helix

19
Q

DNA replication: purpose of RNA primase

A

builds RNA primer

20
Q

DNA replication: purpose of DNA polymerase I, II, III

A

removes RNA primer, adds nucleotides, repairs

21
Q

DNA replication: purpose of ss-binding proteins

A

prevents DNA unwinding

22
Q

DNA replication: purpose of DNA ligase

A

seals gaps in okazaki fragments

23
Q

DNA replication: purpose of sliding clamp

A

keeps DNA polymerase in place

24
Q

DNA replication: purpose of topoisomerase

A

keeps DNA flexible throughout process

25
Q

Describe process of DNA replication

A

1: Helicase unwinds DNA
2: ss-binding proteins stabilize strands
3: leading strand synthesized in 5’-3’ direction using DNA polymerase guided by sliding clamp
4: lagging strand is synthesized discontinously, RNA primase synths a RNA primers which the DNA polymerase binds to to form an okazaki fragment
5:DNA ligase joins okazaki fragments to growing strand

26
Q

About RNA (generic)

A

RNA acts a messenger to create proteins

27
Q

highlights of RNA transcription (enzymes, somponents)

A

RNA polymerase- unwinds dsDNA and copies one strand as RNA
Promoter DNA sequence- binding site for RNA polymerase
Transcription factors- help RNA polymerase find promoter
Termination- releases RNA polymerase and mRNA strand

28
Q

types of RNA

A

mRNA- messenger to encode proteins
rRNA-ribosome components
tRNA- transport amino acids to ribosome
ncRNA- non coding RNA

29
Q

Translation overview

A

Ribosomes read genetic material within mRNA and produce proteins, protein building blocks are amino acids, tRNA transfers amino acids to ribosome

30
Q

About amino acids

A

Codons, or three nucleotides, code for 20 amino acids , many doubles (start codon AUG, stop codons: UAA, UAG, UGA

31
Q

Translation steps

A

initiate, elongate, terminate

32
Q

Components of ribosome

A

large subunit and small subunit, large subunit houses R, P, and A sites

33
Q

How to regulate transcription

A

gene expression refers to mRNA production within the cell, Gene regulation refers to modulating gene expression (transcription factors, activators, enhancer sequences)

34
Q

Two types of genetic mutations

A

SNPs and insertions/deletions

35
Q

what results from SNPs + description

A

Silent- no effect on amino acid sequence
missense- changes amino acid code
nonsense- creates stop codon

36
Q

what results from insertion/deletion and description

A

base pair insertion- frameshift causes entensive missense
frameshift causes immediate nonsense (stop codon)
insertion of deletion of 3 nucleoides-no entensive frameshift

37
Q

define epigenetics

A

changing gene expression in an organism without changing genetic code- environmental factors, methylation, acetylation, phosphorylation

38
Q

describe protein structure/folding

A

proteins develops its structure in 3-4 stages
1: primary protein structure- regular chain
2:secondary- sequence of amino acids is linked by weak hydrogen bonds for fold beta sheets or alpha helixes
3-ternary-when attractions between alpha and beta sheets produce 3-d structures
4-quaternary- a protein of more than one acid chain, consisting of subunits

39
Q

Post translational modifications of proteins

A

chemical groups (methylation, acetylation, phosphorylation), complex grounds (sugars), polypeptides, peptide cleavage, deamidation, can alter protien chanrge hydrophobicity and conformation

40
Q

Enzyme basics

A

large proteins, named by adding -ase to the catalyzed thing, substrate specific, lower activation energies

41
Q

enzyme-substrate interaction

A

bind by weak forces, like hydrogen bonds and vander waals, substrate binds to the active site of the enzyme (lock and key model), maye require co factor or coenzymes

42
Q

what are cofactors and coenzymes

A

grounds added to substrates/proteins, cofactors are ions and coenzymes are proteins

43
Q

what are “Michaelis-Menten” kinetics

A

describe rate of enzymatic reactions, S+E=SE

Introduction to Biotech (1 decks)

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