Task 8: Sequence-based mutation analysis

<css> table.colBasic2 { margin-left: auto; margin-right: auto; border: 2px solid black; border-collapse:collapse; width: 90%; }

.colBasic2 th,td { padding: 3px; border: 2px solid black; }

.colBasic2 td { text-align:left; }

.colBasic2 tr th { background-color:#efefef; color: black;} .colBasic2 tr:first-child th { background-color:#adceff; color:black;}

</css>

Lab journal task 8

Mutation selection

<figtable id="mutations">

Table 1: List of the 10 selected mutations from HGMD and dbSNP.

mutations
nucleotide change	amino acid change
	Val53Met
	His63Asp
	Arg67His
	Met97Ile
	Asn130Ser
	Glu168Gln
	Leu183Pro
	Thr217Ile
	Cys282Tyr
	Arg330Met

</figtable>

Mutation analysis

<figtable id="summary">

Table 2: Summary of the results of analysis of all mutations.

reference	mutation	pyhsicochemical properties		strucural properties		conservation			prediction programms				consensus
		from	to	pymol visualisation	secondary structure	substitution matrix	PSSM	MSA	SIFT	Polyphen2	MutationTaster	SNAP
	Val53Met	brached chain, nonpolar, uncharged	sulfur containing, nonpolar, neutral
	His63Asp
	Arg67His
	Met97Ile
	Asn130Ser
	Glu168Gln
	Leu183Pro
	Thr217Ile
	Cys282Tyr
	Arg330Met			Could not be visualized, because the pdb structure is shorter than the reference sequence and only contains residues residues 22 to 297.

</figtable>

Physicochemical properties are given as special property, side chain polarity and charge.