Assignment of resonances belonging to aromatic residues are important due to several reasons:

• Aromatic residues are frequently found in the hydrophobic part of proteins. Thus, NOEs from them are relevant for protein structure determination.
• Chemical shifts of histidine imidazole rings give information about protonation state, tautomeric structure, solvent accesibility and hydrogen-bonding status.
• The resonance asssignment and NOEs from sidechain part is important to understand protein folding.

     

Experiment	Conditions	Correlation	Related Experiments
2D (HB)CB(CGCD)HD	13C-labeling D2O		3D (HB)CB(CG)CDHD 3D H(CD)CGCB 3D (HB)CB(CGCDCE)HE 2D (HB)CB(Caro)H
3D (HB)CB(C)CaroH	13C-labeling D2O		2D (HB)CB(Caro)H) 3D (HB)CB(CGCDCE)HE
3D HCBCG	13C-labeling D2O		96JMRB259-112
3D (HC)C-(C)CH-TOCSY	13C-labeling D2O		96JMRB259-112
2D H(N)Caro TROSY-based for histidines and tryptophan	13C,15N-labeling		02JB153-22
2D H(CDCG)CB 3D H(CD)CGCB TROSY-based for histidines	13C-labeling		02JB153-22
3D HN(CD)CGCB 2D H(NCDCG)CB TROSY-based for histidines and tryptophan	13C,15N-labeling		02JB153-22
2D and 3D HSQC-TOCSY	13C-labeling D2O		96JB99
2D 15N-filtered 1H-TOCSY	15N-labeling H2O		97JB313
2D 1H-15N Correlations	15N-labelingH2O		Aminoacid-selective 2D correlations 01JMR186-153
HCCCONH experiments for histidine and tryptophan	15N,13C-labelingH2O		05JB309-32
3D HN(CACB)CG and 3D HN(CD)CG experiments for tryptophan	15N,13C-labelingH2O		05JB95-33