Protein structure Flashcards

1
Q

What are the 3 main weak interactions in proteins?

A

1 - Hydrogen Bonds

2 - Van der Waals forces (dipoles between charges)

3 - Hydrophobicity

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2
Q

Describe the 4 levels of protein structure.

A

primary structure - amino acid sequence

secondary - stretches of the amino acid sequence folding up. arrangements of the chain into alpha helices or beta strands

tertiary - collections of linked secondary structure elements fold together in motifs/patterns and these combined form the structure of the complete folded sequence

quarternary - subunits aggregate together top form the biologically active molecule i.e. the Q structure

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3
Q

What is convergent evolution?

A

implies arrival at the same or similar function and/or structure from different starting points

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4
Q

What is divergent evolution?

A

implies a common ancestor, the end result of accumulated mutations in either duplicated genes or diverged species usually being a retention of function and usually a reasonable level of sequence and structural homology.

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5
Q

What are the 2 most common tertiary structure motifs, which are termed domains?

A

alpha-beta domains comprised of a mostly parallel beta sheet flanked by alpha helices

the parallel alpha-beta barrel. a parallel beta barrel surrounded by alpha helices

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6
Q

How is the tertiary structure stabilised?

A

soluble proteins are in their most stable state in water and are stabilised by weak forces such as H bonds, VDW and hydrophobic forces

other forces that stabilise include ionic electrostatic bonds/salt bridges between charged side chains, and disulphide bridges which are formed from the oxidation of 2 cysteine side chains

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7
Q

What does homology mean?

A

the term used to describe the similarities in sequence or structure between 2 or more proteins or genes

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8
Q

What methods are there for determining protein structure?

A

1 - xray crystallography

2 - high resolution electron microscopy

3 - nuclear magnetic resonance

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