I6 Flashcards

1
Q

How does protein crystallograohy work?

A

X-rays hit a protein crystal and hits a detector giving a diffraction pattern which is analysed on a computer.

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2
Q

What is resolution and what is never seen on electron density plots?

A

Electron density contour plots show conc of electrons throughout a molecule
H+ is never seen as there are no electrons present

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3
Q

Explain Abundant, labile and thermodynamically stable

A

Abundant- Can be achieved by expending energy using coupled processes

Labile- Rapid assembly of metal cores and rapid association/dissassociation of substrates

TS- Stable Metal-ligand binds- allow proteins to evolve to bind one type of metal

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4
Q

What is the most abundant TM in biology?

A

Iron 1mg lost per day- Iron storage + transport (transferrin) very efficient!
Iron+Oxygen=free radicals + toxic products

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5
Q

Where is iron stored?

A

Ferretin- Stores 4,500nFe3+ ions
When empty- apoferretin

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6
Q

What protein transports copper?

A

Ceruoplasmin
Made in liver carries 6 Cu ions

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7
Q

What are some factors that affect reduction potential for metal centres?

A

Sigma/pi donors favour high OS and lower reduction potential
Pi-acceptor ligands require low OS and produce high reduction potentials
Changes in metal spin state
Steric factors can favour one OS/spin state - tuning reduction potential by second coordination sphere restricting structural changes

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8
Q

What is Mössbauer Spectroscopy?

A

Only for iron, must be recoilless nuclear resonance adsorption of gamma-radiation. Also has to be solid in ’solid state’ (frozen liquid)
Emitted photon is adsorbed by 57^Fe
Ea-Es= Shift
Transition energy depends on charge density at nucleus

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