Unit 1- Proteins Flashcards

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1
Q

Define allosteric enzymes

A

Enzymes that can change confirmation in response to a modulator

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2
Q

Define a alpha helix

A

Is a polypeptide chain coiled into a helix with hydrogen bonding occurring to maintain the arrangement

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3
Q

Define alternative RNA splicing

A

The removal of non-coding entrance from a primary mRNA transcript to leave only coding exons several mature transcripts can be produced from a single primary transcript

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4
Q

Define beta pleated sheet

A

A polypeptide chain arranged in rows with a chain folding parallel or antiparallel

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5
Q

Define confirmation

A

Structural arrangement of polypeptide chains within a protein it can be altered by factors such as pH on the binding of ligands and modulators

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6
Q

Define cooperativity

A

Changes in finding of a target molecule to one subunit of a multi unit polypeptide changes the affinity of the other subunits for the target molecule

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7
Q

Define disulphide Bridge

A

A strong covalent bond that stabilises the tertairy and quaternary structures of many proteins

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8
Q

Define and endoplasmic reticulum

A

A network of membrane tubules within a cytoplasm of a eukaryotic cell continuous with a nuclear membrane

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9
Q

Define an exon

A

A section of RNA that is usually retain the during splicing

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10
Q

Define a glycoproteins

A

A protein with a carbohydrate added by post-translational modification

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11
Q

Define a golgi apparatus

A

A series of flat and desks that package proteins into membrane-bound vesicles inside the cell before the vesicles are sent to their destination

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12
Q

Define hydrogen bonds

A

Attraction is between polar molecules in which hydrogen is bound to a larger items such as oxygen or nitrogen

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13
Q

Define hydrolylases

A

A class of enzymes that use water to break chemical bonds

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14
Q

Define an intron

A

A section of RNA usually removed during splicing

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15
Q

Define an ionic bond

A

A type of chemical bond that involves an electrostatic attraction between opposite charged ions

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16
Q

Define a ligand

A

A substance that combined to a protein the protein has a shape complimentary to the leg and allowing it to bind

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17
Q

Define London dispersion forces

A

A temporary week attraction between atoms in molecules

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18
Q

Define a lysosome

A

A modified golgi vesicles containing hydrolitic enzymes

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19
Q

Define modulators

A

The spine to the secondary say on the enzyme to alter its confirmation positive modulators activate enzymes negative modulators deactivate them

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20
Q

Define a monomer

A

A molecule that combined chemically to other monomers to form a polymer

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21
Q

Define non-coding RNA gene

A

A gene codes for RNA other than mRNA so do not encode protein

22
Q

Define a phospholipid

A

Component of cell membranes

23
Q

Define a polymer

A

Micro molecule composed of many repeat subunits

24
Q

Define post-translational modification

A

Addition of different chemical groups to or modification of a protein to allow a particular gene function

25
Q

Define a prosthetic group

A

A non-protein unit tightly bound to a protein are necessary for its function

26
Q

Define protein kinesis

A

Catalyse the transfer of a phosphate group from a donor molecule usually ATP to an exceptor

27
Q

Define protein phosphatases

A

An enzyme that removes a phosphate group from its substrate

28
Q

Define protein structure

A

different levels of arrangement of polypeptides within a protein

29
Q

Define primary structure

A

Sequence in which amino acids are found within a protein

30
Q

Define secondary structure

A

Hydrogen bonding occurring within a polypeptide forming alpha helix’s or beta pleated sheets

31
Q

Define tertiary structure

A

Bonding of many types occurring between R groups of amino acids within a protein

32
Q

Define Quaternary structure

A

The arrangement of multiple folded polypeptides connected together

33
Q

Define proteolytic cleavage

A

A major form of post-translational modification it occurs when proteins Cleves one or more bonds in a target protein to activate inhibit or destroy the proteins activity

34
Q

Define a proteome

A

The entire set of proteins expressed by Gino it is much larger than the Ginome

35
Q

Define R group

A

Side groups that allow different bonding between amino acids and give them their wide range of functions

36
Q

Define basic R group

A

Contains and I’m in functional group and produces a basic solution because the extra admin group is not neutralised by the acidic group

37
Q

Define acid R group

A

Contains an acidic function Algroup and produces an acidic solution because the extra acidic group is not neutralised by that I mean group

38
Q

Define polar R group

A

Group that prefers to exist in a watery environment

39
Q

Define hydrophobic R group

A

Composed mainly of carbon and hydrogen is and tend to be repelled from water

40
Q

Define a rough endoplasmic reticulum

A

And organelle made up of membranes with ribosomes attached

41
Q

Define a signal sequence

A

A short stretch of amino acids at one end of the polypeptide that determines its eventual location in the cell

42
Q

What are the roles of kinases and phosphotases

A

Kinases transmit signals to regulate processes they add a negative charge to the protein which can disrupt the ionic interactions

Phosphatases remove phosphate groups and remove the charge from the protein

43
Q

What is the proteome

A

Protein is the entire set of proteins that can be expressed to form a gene

44
Q

Why is the protium larger than the Genome 

A

The pro tube is larger due to its alternative RNA splicing

45
Q

Name the four amino acid R group categories

A

 Basic
 acidic
 polar
Hydrophobic

46
Q

Describe primary protein structure

A

Primary structure is the sequence in which amino acid are synthesise into a polypeptide
Joined by peptide bonds

47
Q

Describe a secondary protein structure

A

Hydrogen bonding on the backbone of the protein Strand results in big games of the secondary structure

Alpha helix a spiral within R group sticking out
Beta pleated sheet and antiparallel also can be parallel
Turns which is polypeptides turn back on themselves

Joined by hydrogen bonds

48
Q

Describe the tertiary protein structure

A

There are regions of secondary structure is stabilised by interactions between different R groups which eachother after folding 

Altogether by hydrophobic hydrophilic London dispersion forces hydrogen bonds ionic bonds and Disulphide bridges

49
Q

Describe quanternary structure

A

Polypeptide has folded into a taxi structure it will join more polypeptides
Held together by hydrogen bonds are in London dispersion forces

50
Q

Describe the conditions which would lower affinity of haemoglobin for oxygen

A

Changes in binding of oxygen at one subject when it’s released from a subunit

Temperature and pH

51
Q

 describe the translation of cytosolic proteins and secrete proteins

A

Synthesis of all protein starts on the cytosolic ribosome the synthesis of the cytosolic proteins is incomplete and the cytosolic ribosomes proteins are released into the size of a move to the rear polypeptide into cinnamon of the rear and post transitional modification begins and go Jefferis protein is packaged into musicals physicals merge proteins

52
Q

Location and forms of post transitional notification

A
Can occur on amino acid sidechains or at the proteins C or N-terminal
Phosphorylation
Glycolisation in the golgi body
Cleveage