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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
CCysCysteine Small Hydrophobic Sulfur containing Helix: – Strand: + Turn: + The SH-group is very reactive: Can make Cys-Cys bridges Can bind metal ions (especially Zn and Cu)
DAspAspartate Intermediately large Hydrophilic Negatively charged Helix: 0 (++ at N-terminus) Strands: – – Turn: ++ Often in active sites Can bind ions (mainly calcium)
EGluGlutamate Large Hydrophilic Negatively charged Helix: ++ Strand: 0 Turn: –
FPhe Phenylalanine Large Hydrophobic Aromatic Helix: 0 Strand: ++ Turn: – –
GGlyGlycine Smallest residue No side chain Hydrophobicity undetermined Very flexible Star of the turn Helix: – – Strand: – Turn: ++
HHisHistidine Large Hydrophilic Charge (depending on the environment): Positive Neutral or Negative No secondary structure preference Often in active sites Can bind metal ions (mainly Zn, Ni, Cu)
IIleIsoleucine Intermediately large Hydrophobic Helix: 0 Strand: ++ Turn: – –
KLysLysine Large Hydrophilic Positively charged Helix: ++ Strand: – Turn: 0 Long, flexible side chain
LLeuLeucine Intermediately large Hydrophobic Helix: ++ Strand: + Turn: – –
MMetMethionine Large Hydrophobic Sulfur containing Helix: ++ Strand: 0 Turn: – – Non-reactive sulfur which can bind metal ions Often the first residue of the sequence
Intermediately large Hydrophilic Helix: – – Strand: 0 Turn: ++ Can bind ions (Ca) but not as well as its isosteric partner Asp NAsnAsparagine
PProProline Small Hydrophobic Helix: – – (except at the first position) Strand: – – Turn: ++ Imino acid No backbone proton Pre-bend for turns
QGlnGlutamine Large Hydrophilic Helix: + Strand: 0 Turn: 0 Isosteric with Glu
Large Hydrophilic Positively charged No secondary structure preference Contains a rigid guanidinium group RArgArginine
SSerSerine Small Intermediate hydrophobicity Alcoholic Helix: – Strand: – Turn: ++ Often in active sites (with Asp and His) Can bind calcium
TThrThreonine Small Intermediate hydrophobicity Alcoholic Helix: 0 Strand: + Turn: 0 Can bind calcium
VValValine Small Hydrophobic Helix: 0 Strand: ++ Turn: – – Isosteric with Thr
WTrpTryptophan Largest residue Hydrophobic Aromatic Helix: 0 Strand: ++ Turn: 0 Most conserved residue
YTyrTyrosine Large Intermediate hydrophobicity Aromatic Alcoholic Helix: – Strand: ++ Turn: 0
Marlou Snelleman 2011 Proteins and amino acids. Overview Proteins Primary structure Secondary structure Tertiary structure Quaternary structure Amino.
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