the 20 amino acids. aalaalanine small hydrophobic helix: ++ strand: – turn: – – mutate to ala...
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![Page 1: The 20 amino acids. AAlaAlanine Small Hydrophobic Helix: ++ Strand: – Turn: – – Mutate to Ala if you have to mutate but have no clue to which residue](https://reader035.vdocuments.mx/reader035/viewer/2022070308/551c2e82550346ad4f8b61fe/html5/thumbnails/1.jpg)
The 20 amino acids
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A Ala AlanineSmallHydrophobic
Helix: ++Strand: –Turn: – –
Mutate to Ala if you have to mutate but have no clue to which residue
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C Cys CysteineSmallHydrophobicSulfur containing
Helix: –Strand: +Turn: +
The SH-group is very reactive:Can make Cys-Cys bridgesCan bind metal ions (especially Zn and Cu)
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D Asp AspartateIntermediately largeHydrophilicNegatively charged
Helix: 0 (++ at N-terminus)Strands: – –Turn: ++
Often in active sitesCan bind ions (mainly calcium)
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E Glu GlutamateLargeHydrophilicNegatively charged
Helix: ++Strand: 0Turn: –
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F Phe PhenylalanineLargeHydrophobicAromatic
Helix: 0Strand: ++Turn: – –
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G Gly GlycineSmallest residueNo side chain
Hydrophobicity undeterminedVery flexibleStar of the turn
Helix: – –Strand: –Turn: ++
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H His HistidineLargeHydrophilicCharge (depending on the environment):
PositiveNeutral or Negative
No secondary structure preference
Often in active sitesCan bind metal ions (mainly Zn, Ni, Cu)
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I Ile IsoleucineIntermediately largeHydrophobic
Helix: 0Strand: ++Turn: – –
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K Lys LysineLargeHydrophilicPositively charged
Helix: ++Strand: –Turn: 0
Long, flexible side chain
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L Leu LeucineIntermediately largeHydrophobic
Helix: ++Strand: +Turn: – –
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M Met MethionineLargeHydrophobicSulfur containing
Helix: ++Strand: 0Turn: – –
Non-reactive sulfur which can bind metal ionsOften the first residue of the sequence
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Intermediately largeHydrophilic
Helix: – –Strand: 0Turn: ++
Can bind ions (Ca) but not as well as its isosteric partner Asp
N Asn Asparagine
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P Pro ProlineSmallHydrophobic
Helix: – – (except at the first position)Strand: – –Turn: ++
Imino acidNo backbone protonPre-bend for turns
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Q Gln GlutamineLargeHydrophilic
Helix: +Strand: 0Turn: 0
Isosteric with Glu
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LargeHydrophilicPositively charged
No secondary structure preference
Contains a rigid guanidinium group
R Arg Arginine
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S Ser SerineSmallIntermediate hydrophobicityAlcoholic
Helix: –Strand: –Turn: ++
Often in active sites (with Asp and His)Can bind calcium
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T Thr ThreonineSmallIntermediate hydrophobicityAlcoholic
Helix: 0Strand: +Turn: 0
Can bind calcium
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V Val ValineSmallHydrophobic
Helix: 0Strand: ++Turn: – –
Isosteric with Thr
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W Trp TryptophanLargest residueHydrophobicAromatic
Helix: 0Strand: ++Turn: 0
Most conserved residue
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Y Tyr TyrosineLargeIntermediate hydrophobicityAromaticAlcoholic
Helix: –Strand: ++Turn: 0