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biology IB > B1.2 Proteins > Flashcards

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

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17
Q

single chain polypeptides=

A

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

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18
Q

why is the structure of a protein important

A

biological function

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19
Q

explain denaturation

A

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

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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

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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

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22
Q

how are amino acids linked together

A

by ribosomes to make polypeptides

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23
Q

what do R groups give each amino acid

A

its unique characteristic present in polypeptide determine properties of assembled polypeptides

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24
Q

R groups which are hydrophobic

A

non- polar repel water molecules

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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

tertiary structure of bonds

A

further folding of polypeptide, dependent of interactions between R-groups, may include; formation of hydrogen bonds, ionic bonds disulphide covalent bonds, hydrophobic interactions
interactions stabilise structure of protein, produces overall rise of 3d shape of protein

31
Q

tertiary structure- hydrogen bonds

A

between polar R-groups in tertiary structure of a protein; crucial role in stabilising 3D shape by holding distant regions of polypeptide chain together, stabilising effect crucial for maintaining proteins functional integrity and any slight deviations from correct structure can impair activity of protein

32
Q

tertiary structure- ionic bonds

A

type of chemical bond between opositely charged ions
in protein r-groups can undergo binding or dissociation of hydrogen ions results in positive or negative charged state
charged r-groups can then interact with oppositely charged atoms in other molecules forming ionic bonds, ionic bonds can further contribute to overall stability and function of protein

33
Q

tertiary structure- disulphide covalent bonds

A

form between pairs of cysteine amino acid residues, contain sulfur atoms
bonds critical stabilising tertiary and quaternary structures of proteins by forming covalent bonds help maintain proteins overall 3D shape, contributing to stability and function

34
Q

tertiary structure- hydrophobic interactions

A

occur between non-polar amino acids, occurs as water is a polar molecule and forms hydrogen bonds with polar amino acids
as non-polar amino acids are unable to interact with water, tend ti clump together into hydrophobic clusters in interior of protein to minimise contact with surrounding water molecules. hydrophobic interactions stabilise proteins tertiary and quaternary structure

35
Q

how do Hydrophilic polar amino acids orient

A

orient to the outside towards the aqueous environment

36
Q

how do hydrophobic non-polar amino acids

A

are protected in the core, minimising unfavourable interactions between hydrophobic side chains and water molecules.

37
Q

how do polar and non polar amino acids affect structure of proteins

A

The resulting compact, folded conformation exposes hydrophilic surfaces to the solvent and buries hydrophobic residues in the protein’s interior, thereby contributing to protein stability and function

38
Q

mygoblin

A

A protein found in muscle tissue that binds and stores oxygen.

39
Q

haemoglobin

A

The iron-containing protein present in red blood cells that carries oxygen.

40
Q

globular proteins

A

Proteins that are compact and spherical in shape. They play important roles as enzymes, transporters and regulators.

41
Q

what do integral proteins also have

A

regions with hydrophobic amino acids, helping them to embed in membranes

42
Q

what does the function of a protein arise from

A

uniqeu structure

43
Q

what controls the number of different protein levels

A

depending on the number and types of interactions between the amino acid residues within the protein chain

44
Q

quaternary structure

A

Structure of a protein refers to the arrangement and interaction of two or more polypeptide chains to form a functional protein. eg. haemoglobin

45
Q

hameoglobin describe structure

A

which consists of four individual polypeptide chains: two of which are designated ‘ɑ-chains’ and two which are designated ‘β-chains’, its a conjugated protein which contains Haem, is a complex molecule with iron in its centre. It is responsible for binding to oxygen in the lungs and facilitates the transport of oxygen throughout the body.

46
Q

conjugated proteins

A

Proteins that contain a non-protein component such as a metal ion or a carbohydrate.

47
Q

explain oxygens four subunits, its importance

A

The four subunits of haemoglobin are held together by non-covalent bonds, and the interactions between the subunits allow haemoglobin to undergo conformational changes necessary for its oxygen-carrying function

48
Q

why is the quartenary structue of protein important

A

The quaternary structure of haemoglobin is essential for its biological function and highlights the complexity and importance of protein structure in biological systems.

49
Q

non conjugated proteins

A

Proteins that consist only of amino acids linked together by peptide bonds. eg. collagen, insulin

50
Q

conjugated proteins

A

have non-protein components such as metal ions or carbohydrates in addition to having polypeptide subunits. These non-protein components have the ability to increase a protein’s diversity and functionality. For example, non-protein components play a crucial role in many enzymes, helping them perform their catalytic functions.

51
Q

Differences in shape, solubility and function are due to…

A

due to differences in the amino acid composition and the way the polypeptide chains are folded and arranged.

52
Q

what happens After a polypeptide chain is synthesised

A

t undergoes a process called protein folding in which it adopts a specific three-dimensional shape that is critical for its proper function

53
Q

The protein folding process is influenced by

A

various chemical and physical forces, such as hydrogen bonding, ionic bonding and hydrophobic interactions, and is determined by the sequence of amino acids in the protein as well as the cellular environment in which it is synthesised. Once proteins take their final form, they can be classified as either globular or fibrous.

54
Q

explain a bit about structure of insulin

A

consists of two polypeptide chains: the ɑ-chain and β-chain (Figure 2). They are arranged in a specific three-dimensional shape that is held together by hydrogen bonds, hydrophobic interactions and disulfide bonds.

55
Q

insulin role

A

A hormone that regulates glucose levels in the bloodstream by facilitating glucose uptake and storage in cells.

56
Q

whats the overall structure of insulin

A

compact and globular with a hydrophilic exterior and a hydrophobic interior.

hydrophilic exterior allows insulin to interact with water and other hydrophilic molecules in the blood. This is important because insulin needs to travel through the bloodstream to reach its target tissues, and bind to its receptors.

hydrophobic interior of the insulin protein helps to stabilise the shape of the protein, allowing it to maintain its globular shape, which is essential for the insulin to bind to its receptor.

57
Q

fibrous proteins

A

Structural proteins that have an elongated shape. usually composed of repeating structures that are designed for strength and stability and are insoluble in water. Fibrous proteins provide structural support and stability to cells and tissues such as skin, tendons, and bone.
for example collagen

58
Q

collagen role

A

A fibrous protein that provides strength and support to various tissues in the body, including bones, tendons and cartilage

59
Q

talk about structure of collagen

A

made up of three polypeptide chains that are twisted together in a triple helix structure
Each chain is rich in the amino acid glycine, and it contains many proline and hydroxyproline residues.
residues allow the chains to twist together into a tight helix that is held together by hydrogen bonds and van der Waals forces

60
Q

why is the triple helix of collagen important

A

triple helix structure of collagen is long and thin, giving collagen fibres their characteristic elongated fibrous shape. The fibres are very strong and flexible, resisting forces without breaking. This provides structural support to tissues, helping them to maintain their shape and integrity.

biology IB (8 decks)

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