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Amino Acids (NMR and more)

Random Coil chemical shifts (short overview) of some selected atoms

13C chem. shift Cα 13C chem. shift Cβ
 Diagramm1  Diagramm2
13C chem. shift C=O 15N chem. shift NH
 Diagramm3  Diagramm4
 h-alpha  h-beta

Sources:
David S. Wishart, Colin G. Bigam, Arne Holm, Robert S. Hodges, Brian D. Sykes; Journal of Biomolecular NMR
January 1995, Volume 5, Issue 1, pp 67-81 doi:10.1007/BF00227471

More details

nonpolar/hydrophobic alkaline
Tryptophan

Tryptophan (W, Trp)

Valin

Valine (V, Val)

Alanin

Alanine (A, Ala)

Isoleucin

Isoleucine (I, Ile)

Leucin

Leucine (L, Leu)

phenylalanin

Phenylalanine (F, Phe)

Prolin

Proline (P, Pro)

 

Methionin

Methionine (M, Met)
Arginin

Arginine (R, Arg)

Histidin

Histidine (H, His)

Lysin

Lysine (K, Lys)
polar/neutral acidic
Tyrosin

Tyrosine (Y, Tyr)

asparagin

Asparagine (N, Asn)

Glutamin

Glutamine (Q, Gln)

Cystein

Cysteine (C, Cys)

Glycin

Glycine (G, Gly)

Serin

Serine (S, Ser)

Threonin

Threonine (T, Thr)
Asparaginsäure

Aspartic acid (D,Asp)

Glutaminsaeure

Glutamic acid (E, Glu)

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Chemical Shift Index (Secondary structure of Amino Acids)

The formation of the chemical shift index is a method to determine the secondary structure of proteins from the chemical shifts of backbone atoms. It is based on the chemical shifts listed in the following table (+- 0.7ppm). The following simple rules are applied: 1 is assigned if the measured chemical shift is greater than …