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Biomed year 2 > Huabing (Block 1 ENG in Bio) > Flashcards

Huabing (Block 1 ENG in Bio) Flashcards

1
Q

What is a hydrogen bond ?

A

A polar interaction in which an electropositive hydrogen atom is
partially shared by two electronegative atoms

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2
Q

What is a ionic bond ?

A

Attractive forces between oppositely charged atoms

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3
Q

What is a covalent bond ?

A

Formed by the sharing of electrons

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4
Q

What is Van der Waals attraction ?

A

the interaction between opposite dipoles of atoms

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5
Q

What is the use of Hydrophobic force for bonding ?

A

Is not a bond, but caused by a pushing of nonpolar surfaces out of the
hydrogen-bonded water network

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6
Q

Typical covalent bonds are stronger than thermal energy by a factor of ?

A

100 therefore not easily pulled apart by heating

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7
Q

What type of bonds specify the precise shape of a macromolecule ?

A

Non-covalent

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8
Q

What is a macromolecule ?

A

A macromolecule is a very large molecule, such as a protein. They are composed of thousands of covalently bonded atoms. … The most common macromolecules in biochemistry are biopolymers (nucleic acids, proteins, and carbohydrates) and large non-polymeric molecules such as lipids and macrocycles

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9
Q

What form of movement do covalent bonds allow in a macromolecules and how is this countered ?

A

Rotational, countered by many non-covalent bonds to hold in place

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10
Q

What bonds link amino acids together and what is what is forms called ?

A

Covalent peptide bonds, together form the polypeptide backbone.

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11
Q

What determines the precise shape of a protein ?

A

It’s amino acid sequence

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12
Q

What does the side chain do in a protein ?

A

The side chain gives each amino acid

unique properties and are involved in forming noncovalent bonds to help proteins fold.

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13
Q

What 3 types of non-covalent bonds are used in protein folding ?

A

Van der waals , Hydrogen bonds and electrostatic bonds (ionic bonds ).

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14
Q

What force can be involved in protein folding ?

A

Hydrophobic forces (when in water ).

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15
Q

Proteins generally fold into a shape in which _____ is minimised ?

A

Free energy

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16
Q

What are the most structurally diverse macromolecules in the cells ?

A

Proteins

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17
Q

What are the 2 most regular folding patterns for proteins ?

A

Alpha helix and the beta sheet

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18
Q

What is the primary structure of a protein ?

A

It’s amino acid sequence

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19
Q

What is the secondary structure of a protein ?

A

Alpha helices and beta sheets that form within certain segments of the polypeptide chain.

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20
Q

What is the tertiary structure of a protein ?

A

The full 3D conformation, is formed

by an entire polypeptide chain, including the alpha helices, beta sheets, and any other folds

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21
Q

What is the quaternary structure of a protein ?

A

The complete structure of a protein ,if the protein is formed out of several polypeptide chains.

22
Q

What is a Protein domain ?

A

A protein domain is defined as any segment of a

polypeptide chain that can fold independently into a compact, stable structure

23
Q

What is a protein family ?

A

proteins consisting of similar amino acid sequences and 3D conformation are unusually
grouped as a protein family

24
Q

Larger protein molecules often contain more than one polypeptide chain. Any region on a protein surface that has this capability is termed?

A

A binding site

25
Q

Each peptide chain in a large protein with multiple chains is called ?

A

A subunit.

26
Q

In addition to the non-covalent bonds, ___________ between polypeptide chains are often formed to reinforce the structure of proteins (name the most common )

A

covalent cross-linkages (Disulfide)

27
Q

Any substance that is bound by a protein is referred to as a ______ for that protein

A

Ligand

28
Q

Each antibody can recognize and bind to a particular target (called an _______) extremely tightly

A

antigen

29
Q

What shape is an Antibody ?

A

Y shaped

30
Q

Antibodies are formed from four __________ held together by ________ bonds: two are identical ______
chains and two identical _______ chains.

A

1 .Polypeptide chains

  1. disulfate
  2. heavy
  3. light
31
Q

The antigen binding site of an antibody is formed by ?

A

Close association of variable domains from heavy and light chains.

32
Q

Antigen binding site complementary to a site on the antigen (known as the ________) in terms of shape and the arrangement of ________ and _______ groups

A
  1. epitome
  2. hydrophobic
  3. charged
33
Q

The movements of protein machines is coordinated by what ?

A

The hydrolysis of a bound nucleoside triphosphate (ATP or GTP).

34
Q

What does the plasma membrane do ?

A

Acts as a selective barrier to maintain a constant intracellular composition

35
Q

The ___________ senses the external signals and allows the cell to change its behavior in response to the signals

A

plasma membrane

36
Q

What makes up the lipid bilayer ?

A

Lipids arranged in two closely apposed sheets. The hydrophilic heads are attracted to the water molecules and the hydrophobic repel.

37
Q

What does the lipid bilayer do ?

A

Serves as a permeability barrier to most water-soluble molecules

38
Q

Describe a lipid molecule

A

A hydrophilic head and 1 or 2 hydrophobic hydrocarbon tails known as amphipathic

39
Q

The fluidity of the lipid bilayer depends on what ? And explain how this effects fluidity

A

On it’s composition, the more closely packed the hydrocarbon tails are the more viscus and less fluid the bilayer becomes

40
Q

Read from lecture 4 slide 9 to end These are hard to question on without images.

A

I did it .

41
Q

Name the 4 types of signaling between cells

A

Endocrine signaling ,paracrine signaling, neuronal signaling,contact-dependent signaling.

42
Q

Describe endocrine signaling

A

Endocrine cells secrete hormones into the bloodstream, affecting the target cells anywhere in the body

43
Q

Describe paracrine signaling

A

The signal molecules diffuse locally through the

extracellular fluid, acting as local mediators

44
Q

Describe neuronal signaling

A

Neuron cells can deliver electrical signals over long distances

45
Q

Describe contact-dependent signaling

A

The signal molecules on the surface of the signaling cell are in direct physical contact with the receptor
proteins on the surface of the target cells

46
Q

Name and describe the 2 classes of receptor

A 
1. The first and largest class rely on cell-surface receptors to relay their message across the plasma
membrane.
  1. The second class are generally small and hydrophobic molecules that can diffuse through the membrane. Once inside they usually bind to intracellular receptors.
47
Q

What regulates the activity of specific intracellular proteins ?

A

Nitric oxide

48
Q

Many key intracellular signaling proteins behave as __________?

A

Molecular switches

49
Q

Describe and draw protein phosphorylation and signalling by GTP

A

Found on block 1 L5 slide 7

50
Q

What are the 3 families of cell-surface receptors ?

A

Ion-channel coupled receptors,G-protein-coupled receptors, enzyme-coupled receptors

51
Q

What are ion-channel-coupled receptors responsible for and what do they do ?

A

They are responsible for the rapid transmission of signals across synapses in the nervous system and they convert chemical signals into electrical ones

52
Q

Read Block 1 L5 silde 9-15

A

DONE ?

Biomed year 2 (7 decks)

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