B1.2 Proteins Flashcards

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1
Q

how is the generalised amino acid

A

it is composed of a variable group, carboxyl groups, amine group

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2
Q

what are the 4 groups in which the 20 amino acids are organised into

A
  1. non- polar side chains= hydrophobic will contain either just a h or ch as a variable group
  2. polar side chains, hydrophilic can either have an oxygen in ending except 1 sulfur in cys
  3. electrically charged side chains
    - acidic= negative charge
    - basic= positive charge
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3
Q

explain each of 20 amino acids

A

each have different R-groups can be polar or non-polar linear or ringed; distinct chemical and physical properties

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4
Q

what do condensation reactions form

A

dipeptides and longer chain amino acids
the peptide bond forms when carboxyl group of one amino acid reacts with the amine group of another forming a dipeptide and water is a byproduct
peptide bond= covalent bond which is very stable
even longer chain amino acids= polypeptides

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5
Q

what are essential amino acids

A

amino acids the body cant produce must obtain through diet
necessary for growth, maintenance and repair of bodys tissues and organs

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6
Q

what are non essential amino acids

A

produced by body from other amino acids or by breakdown of protein

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7
Q

what is a genetic code

A

set of rules which specifies how info is stored in dna is translated into sequence of amino acids that make up proteins
->provides instructions for protein synthesis through processes of transcription and translation

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8
Q

what is transcription

A

dna transcribed- mrna

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9
Q

what is translation

A

mrna translated into sequence of amino acids

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10
Q

genetic code is composed of

A

codons, groups of 3 nucleotides specify type of amino acid or stop signal required

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11
Q

how is it possible to be 64 different codons but only 20 amino acids

A

degenerate some amino acids coded for by multiple coded for by multiple codons allows possibility silent mutations= change DNA sequence not result in change in amino acid sequence of protein

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12
Q

what is the infinite variety peptide chains

A

ability combine 20 dif amino acids in any sequence

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13
Q

what is a polypeptide

A

chain of amino acids linked by peptide bonds

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14
Q

what is a protein

A

a complex 3d structure made of 1 or more polypeptide chains

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15
Q

explain protein composed 1 polypeptide chain

A

amino acids interact with each other folding chain into a functional protein

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16
Q

explain protein composed of more than one polypeptide

A

polypeptide chain can additionally interact with each other contributing overall structure of protein

17
Q

single chain polypeptides=

A

function; enzymes and hormones, molecules possess specific primary structure= linear sequence of amino acids that make up protein

18
Q

why is the structure of a protein important

A

biological function

19
Q

explain denaturation

A

process structure protein altered cause loss function; usually permanent
ph and temp can cause

20
Q

what can extreme change in ph affect

A

protein solubility and shape; altering proteins change- leads irreversible changes in protein structure cause inactivity

21
Q

what can high temp cause in proteins

A

can break weak hydrogen bonds holding protein structure together, cause protein to unfold and lose function

22
Q

how are amino acids linked together

A

by ribosomes to make polypeptides

23
Q

what do R groups give each amino acid

A

its unique characteristic present in polypeptide determine properties of assembled polypeptides

24
Q

R groups which are hydrophobic

A

non- polar repel water molecules

25
Q

R groups which are hydrophilic

A

polar or charged, acidic or basic, attract water molecules

26
Q

what do polar R groups contain

A

partial charges that interact with water molecules while charged R-groups can be positive charged (basic) or negative charge (acidic)

27
Q

how many levels are there of protein structure

A

4

28
Q

describe primary structure of proteins

A

specific sequence of amino acids joined together from polypeptide chain
determines how polypeptides chain will fold, leading to 3d structure protein precise position each amino acid within protein is critical determing its shape

29
Q

describe secondary structure of proteins: pleating and coiling

A

folding patterns that occur within polypeptide chain common type secondary structure; alpha helices and beta-pleated sheets
ability fold into coils and pleats achieved through hydrogen bonding between carboxyl group and amino acid in different part of polypeptide chain. Hydrogen bonds occur regular positions help stabilize and aid in formation of secondary structure
collectively hydrogen bonds= strong, hold confirmation of protein
alpha helix hydrogen bonds from between amine hydrogen 1 amino acid and carboxyl oxygen from another amino acid 4 residues away in sequence, repeated pattern allows polypeptide chain to coil- helical structure
beta pleated sheets form sections polypeptide chain run parallel each other hydrogen bonds form between adjacent strands, individual strands forming flat surface of the sheet

30
Q
A