Protien Molecules Flashcards

(46 cards)

1
Q

What bonds are amino acids linked by

A

Covalent bonds in linear chain

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2
Q

Primary structure of proteins

A

Linear amino acid sequence

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3
Q

Secondary structure of proteins

A

Polypeptide folding into regular shapes (forms domains)

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4
Q

Tertiary protein structure

A

Arrangement of one or more domains (3D structure)

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5
Q

Quaternary protein structure

A

Arrangement of multiple polypeptide chains in one protein - forms protein complex with subunits

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6
Q

What are domains

A

How elements of secondary structure are packed together

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7
Q

What is the alpha carbon in an amino acid

A

Linked to amino group (-NH2), a carboxyl group (-COOH), a alpha hydrogen atom and an R group (chiral carbon)

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8
Q

What form do amino acids exist in neutral pH

A

Zwitterion form at neutral pH

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9
Q

What does the formation of a dipeptide from two amino acids results in

A

Loss of water - condensation reaction

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10
Q

What is a residue

A

Each amino acid unit of polypeptide chain called a residue

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11
Q

What structure do peptide bonds adopt

A

Rigid planar structure

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12
Q

How are disulphide bonds formed

A

Between side chains of two cysteine residues under oxidising conditions

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13
Q

How can disulphide bonds be cleaved

A

By reducing agents such as B (beta) - mercaptoe thanol

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14
Q

What are histones composed of

A

DNA packaging - many Arg, Lys => very basic proteins

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15
Q

What are membrane proteins composed of

A

Many Leu, Val and ile = > hydrophobic proteins

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16
Q

What amino acids compose extracellular proteins

A

Many Cys to form disulphide bond, stable protein

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17
Q

What is a result of cis configuration of side chains

A

Neighbouring amino acids can result in steric hinderance

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18
Q

Types of non covalent bonds

A

Hydrogen bonds
Salt bridges (electrostatic interaction)
Vẫn đẻr waals interaction

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19
Q

What are Hydrogen bonds essential for

A

Crucial for protein folding and formation of secondary structure

20
Q

Formation of salt bridges and their importance

A

-Formed by attractive forces between oppositely charged atoms
- important in quaternary structure formation

21
Q

Where do Hydrogen bonds form on secondary structure of protein

A

Between -Nh and -CO groups on different but adjacent strands

22
Q

What are the two main secondary structures of a protein

A

Alpha helixes (a-helices)
Beta sheet (B-sheet)

23
Q

What are tertiary structures composed of

A

‘Bundles’ (aka domains) of secondary structures

24
Q

Characteristics of a domain

A

-hydrophilic side chains exposed
-hydrophobic side chains buried in hydrophobic core

25
What is a domain
Region of polypeptide chain that folds independently and self stabilising
26
How do polypeptide chains fold
Fold spontaneously in aqueous environment
27
What does the hydrophobic effect drive
Drives formation of hydrophobic core proteins and promotes tertiary structure formation
28
What are the 3 classes of domain structures
-alpha helical domains -beta sheet domains -alpha/beta domains
29
Characteristics of alpha helical domains
packed together in bundles or ‘coiled -coil’
30
What do common domains consist of
-pair of helices -connected by short loop -packed in anti parallel arrangement
31
What is a beta sandwich and it’s characteristics
-two beta sheets packed together -stabilised by ‘fillings’ - hydrophobic side chains
32
What is the B - barrel and its characteristics
-eight b -strands may form closed ‘barrel’ structure (Chinese finger trap looking like) Hydrophobic residues orientated towards centre of barrel
33
What is the Ross man fold
Beta strand and alpha helical repeats
34
In clonal selection what happens to activated B cells
B cell clone will proliferate and differentiate into antibody secreting cells
35
What is innate immunity
Rapid but non-specific
36
What is adaptive immunity
Based on lymphocyte with antigen receptors - immunological memory
37
What is the epitope
The antigenic determinant and site where antibody binds to on the antigen
38
What is neutralisation in immunity
Binding of antibodies to epitope on surface of pathogens prevents entry to host cells
39
What is opsonisation in immunity
The coating of a pathogen with molecules like antibodies and increases efficiency of phagocytosis
40
What agglutination in immunity
The process of the clumping of pathogens driven by interaction of antibody with antigens and prevents spread of pathogens through the system
41
What is the complement cascade in immunity
Antibody-antigen complex stimulates binding of Cl => activation of protease that triggers chains of amplification cascade
42
What is antibody dependant cellular cytotoxicity in immunology
Mechanism where large pathogens are killed by secretion of cytotoxic
43
What is the stimulation of cytokine release in immunology
IgE antibodies bind to receptors on mast cells and basophils => antigen binding to IgE on these cells stridulate the secretion of cytokines and histamine
44
What does histamine do
Causes vasodilation and leafiness in blood vessels - its release causes allergic reactions
45
What are IgE antibodies produced in response to
Response to parasites and environmental allergens e.g pollen, food and drugs
46
What is the structure of immunoglobulin (Ig)/antibody)
-4 polypeptide chains - two heavy (H) chains - two light (L) chains -linked by disulphide bonds