Lecture 3 Flashcards

1
Q

What’s uniprot

A

Another helpful website to show the properties of proteins that you search

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2
Q

What websites are used to predict tertiary structure of proteins

A

Alpha fold and Rosettafold

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3
Q

What types of confidence score does alpha fold provide

A

A per residue score between 0 and 100

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4
Q

What score is accurate

Good prediction of backbone

Low confidence

Correlated with disorder

A

> 90

70-90

50-70

<50

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5
Q

What does cryoEM help with

A

To see complexes between proteins

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6
Q

What type of experimental method contributes most to finding the structure of proteins in the PDB

A

CryoEM

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7
Q

What do we used to predict/calculate proteins properties

A

Expasy-peptide mass

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8
Q

What is the pI of a protein

A

The pH where the not charge of the protein is zero

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9
Q

What is the pI of a protein

A

The pH where the net charge of the protein is zero

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10
Q

Why is tryptophan’s usually low in the amino acid composition of proteins

A

Because it has a specific role

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11
Q

How do pyrrolysine and selenocysteine get formed

A

Instead of a stop codon, they get formed

They come from stop codons

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12
Q

What are the units of extinction coefficients

A

M-1cm-1

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13
Q

How do you calculate the extinction coefficient if a protein

A

(#tyr x extinction of tyr) + ( #trp x extinction of trp) + (#cystine x extinction of cystine)

Not cys, cystine (disulphide bond)

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14
Q

What is tyr
Trp
Cystine

Extinction coefficient

Which dominates the equation

A

1490

5500

125

Trp

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15
Q

How can you calculate the absorbance (optical density) of a protein

A

It’s total calculated extinction coefficient/ MW

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16
Q

Why do we use cystine and not cystieine when doing the extinction coefficient calc

A

Because only cystine absorbs a 280nm

17
Q

What is quaternary structure

A

Two protiens form a complex

18
Q

What websites are use to analyze quaternary structure of protiens

A

Rosetta fold 3 and alpha fold 3

19
Q

What do the websites that analyze quaternary structure actually look at

A

The interface area

The hydrogen bonds

Salt bridges

The hydrophobic surface