Bio (12): Amino acid codon table............

#CODON TABLE (Most amino acids are represented by 2 codons)
Alanine (Ala) (A): GCA, GCC, GCG, GCT---4---GCN
Arginine(Arg) (R): CGT, CGC, CGA, CGG, AGA, AGG---6---CGN, MGR
Asparagine(Asn) (N): AAT, AAC---2---AAY
Aspartic acid(Asp)(D): GAT, GAC---2---GAY
Cysteine(Cys)(C): TGT, TGC---2---TGY
Glutamine (Gln)(Q): CAA, CAG---2---CAR
Glutamic acid (Glu)(E): GAA, GAG---2---GAR
Glycine (Gly)(G): GGT, GGC, GGA, GGG---4---GGN
Histidine(His) (H): CAT, CAC---2---CAY
Isoleucine(Ile) (I): ATT, ATC, ATA---3---ATH
Leucine(Leu) (L): TTA, TTG, CTT, CTC, CTA, CTG---6---YTR, CTN
Lysine(Lys) (K): AAA, AAG---2---AAR
Methionine (Met) (M): ATG---1
Phenylalanine(Phe) (F): TTT, TTC---2---TTY
Proline(Pro) (P): CCT, CCC, CCA, CCG---4---CCN
Serine(Ser) (S): TCT, TCC, TCA, TCG, AGT, AGC---6---TCN, AGY
Threonine (Thr) (T): ACT, ACC, ACA, ACG---4---ACN
Tryptophan (Trp) (W): TGG---1
Tyrosine (Tyr) (Y): TAT, TAC---2---TAY
Valine (Val) (V): GTT, GTC, GTA, GTG---4---GTN
*STOP TAA, TGA, TAG---3---TAR, TRA
#Asn, Leu, Ser have six codons
#Met and Trp have 1 codon each
Polar amino acids
Glutamine - Gln - Q 
Asparagine - Asn - N 
Histidine - His - H 
Serine - Ser - S 
Threonine - Thr - T 
Tyrosine - Tyr - Y 
Cysteine - Cys - C 
Methionine - Met - M 
Tryptophan - Trp - W 

Non-polar (aliphatic or aromatic) amino acids
Alanine - Ala - A 
Isoleucine - Ile - I 
Leucine - Leu - L 
Phenylalanine - Phe - F 
Valine - Val - V 
Proline - Pro - P 
Glycine - Gly - G

Charged amino acids
Arginine - Arg - R 
Lysine - Lys - K 
Aspartic acid - Asp - D 
Glutamic acid - Glu - E 

Essential amino acids (9): Phenylalanine, valine, threonine, tryptophan, methionine, leucine, isoleucine, lysine, and histidine (F V T W M L I K H)

Conditionally-essential amino acids (6): Arginine, cysteine, glycine, glutamine, proline and tyrosine (R C G Q P Y)

Non-essential amino acids (5): Alanine, aspartic acid, asparagine, glutamic acid and serine (A D N E S)

* This chart retrieved from http://www.sigmaaldrich.com/ is useful
Proteins have a hydrophobic core and hydrophilic surface(to form hydrogen bond with water).
So, if a surface protein becomes hydrophobic, protein can't interact with water and looses stability.