lecture 2🅱️ Flashcards

1
Q

what happens during induced fit

A

the target changes shape in order to bond more tightly,, this shortens bond,, making it stronger

stronger binding interaction due to induced fit

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2
Q

what are the building blocks of protein

A

amino acids

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3
Q

what do amino acids possess on the same c atom

A

they have an
amine
carboxylic acid

on the same carbon

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4
Q

charge of amine on aa

A

NH3
+

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5
Q

charge of carboxylic acid on aa

A

COO -

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6
Q

amine + carboxylic acid form which bond

A

amide bonds

peptide bonds

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7
Q

are the NH3+ or COO- ever seen

A

only on terminal amino acids.

theyre normally present as peptide bonds

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8
Q

most important group of an amino acid

A

the R group.
its unique

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9
Q

what elements are present in amino acids

A

C,O,S,H,N

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10
Q

what does amino acid classification depend on

A

depends on the R group or the side chain.

same thing different name

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11
Q

classification of amino acids

A
  • non polar,, aliphatic
  • aromatic
  • polar,, uncharged
  • positively charged
  • negatively charged
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12
Q

non polar + aliphatic can give what bonds

A

VDW
hydrophobic

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13
Q

polar // uncharged aa can give what bonds

A

DD, hydrophilic,, H bonding

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14
Q

positively and negatively charged aa can give what bond

A

ionic bonds

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15
Q

hydrogen bond donor

A

NH2
OH
FH

electronegative atom covalently bonded to a H

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16
Q

hydrogen bond acceptor

A

electronegative + lone pair
not covalently bonded to a H.

C=O

17
Q

name 3 structural biology techniques

A
  • NMR
  • x ray crystallography
  • neutron diffraction
18
Q

what is xray crystallography

A

using crystals to diffract an xray in order for the diffraction pattern to be detected (xray detector) to give an electron density map (using computers + graphics) and therefore a secondary protein structure.

19
Q

what is a limitation of xray crystallography

A

the object must be crystallised.

in order for the bonds to be a certain distance

so they can defract X-rays.

protons cannot be seen - no h bonds

static picture: crystal packing forces may affect the structure observed

20
Q

positives about xray crystallography

A

atomic scale picture is very accurate

must important structural biology technique

crysal structure data gives coordinates and there can be used as a starting point for computer modelling/ simulations

21
Q

why does the crystal have to be 3d + crystallised

A

the diffraction pattern must be collected for the whole crystal structure:: the crystal must be turned 360* to allow a complete diffraction pattern

22
Q

what does nmr stand for

A

nuclear magnetic resonance

23
Q

are all nmrs 1d

A

nope!!
1d
2d
3d

24
Q

negatives for nmr

A

smaller proteins only!!

size limitation

25
Q

positives for nmr

A
  • doesnt need to be a crystal
  • atomic scale picture is very accurate
    -u can see protons
  • dynamic picture given (can be in solution - not crystalline)
  • can be used as a starting point for computer modelling / simulations
26
Q

5 key features of amino acids

A
  • alpha amino acids: all possess amine and carboxylic acid on the same carbon atom
  • possess a side chain on each carbon (except glycine)
  • linked to form polymers (proteins) using the alpha amino and carboxylic acid
  • possess 5 elements: N O C H S
27
Q

4 key features of amino acids

A
  • alpha amino acids: all possess amine and carboxylic acid on the same carbon atom
  • possess a side chain on each carbon (except glycine)
  • linked to form polymers (proteins) using the alpha amino and carboxylic acid
  • possess 5 elements: N O C H S
28
Q

NMR steps

A
  • labelled proteins
  • data acquisition
  • spectroscopy processing
  • computer simulations