Lecture 4 Bioinformatics Flashcards

0
Q

Homology

A

Like one another

We will deal with sequence homology, especially proteins

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1
Q

Bioinformatics

A

Exploded over last ten years

Sequence information

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2
Q

2 classes of homologs

A
  1. Paralogs - within species

2. Orthologs - Similar functions in different species

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3
Q

Paralogs

A

Within species, similar to each other

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4
Q

Orthologs

A

Similar functions in different species

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5
Q

Protein domains

A

Many proteins have single domains, some have lots.

Ex. Titan, 300+ domains

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6
Q

Hemoglobin VS. Myoglobin

A

Function is binding and transporting O2
VS. Reversible binding for O2, no transport in myoglobin
Compare the two sequences.
Sliding and Shuffling

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7
Q

2 Types of Sequence Alignment

A
  1. Sliding Alignment - slide along and see where they match
  2. Shuffling - take sequence and shuffle them
    * Blosum 62 Substitution Matrix
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8
Q

Sliding Alignment

A

Slide sequences along each other and see where they match.
Ex. NCBI has Blast program that does this
Gives a simple score, can be 0-10

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9
Q

Shuffling Alignment

A

Take sequence and shuffle them (need high powered computer to do this)
Blosum 62 Substitution Matrix (25 varieties)
Gives scoring mechanism to look at chances for mutations
Scoring of conservative and nonconservative substitutions

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10
Q

Blosum 62

A

Substitution Matrix (shuffling alignment)
Scoring mechanism to look at changes for mutations
Minus score - the more negative, the more unlikely they are to occur
Ex. cysteine and tryptophan NOT favorable
Can distinguish between conservative and nonconservative

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11
Q

Substitution Matrix

A

Ex. Blosum 62

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12
Q

Branch chain AA are generally

A

interchangeable

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13
Q

Negative score on Blosum 62

A

Nonconservative

The more negative, the more unlikely to occur

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14
Q

Two AA that almost never mutate

A

Cysteine and Tryptophan (W)

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15
Q

Positive score on Blosum 62

A

Conservative substitution

Likely to occur

16
Q

Hypervariable

A

5 that you compare, none are the same, tells you region of protein is not important for sturcture or function

17
Q

If conserved over species

A

you know area is imp for structure/function of protein

18
Q

Conservative substitution

A

Receives a positive score

Ex. Lysine for arginine

19
Q

Nonconservative substitution

A

Is scored negatively

Ex. Lysine for tryptophan

20
Q

BLAST

A

program by ncbi

Compares two sequences using sliding anaylsis

21
Q

Letter in middle of two sequences

A

Same

22
Q

+ sign in middle of two sequences

A

Positive, highly conserved

Frequent substitution

23
Q

Space in middle of two sequences

A

Not conserved