Applications

Recognition of protein folding ( 99JB223-14 , 00JMB447 and 03JB63-25).

Study of the relative domain orientation ( 99BIO9013 , 00JMB1265 , 01JMB745 , and 01JACS8634 )

Analysis of anisotropic small amplitude peptide plane dynamics ( 04JACS4907 )

Determination of relative orientation in a dimer from ¹D_NH ( 00JACS6009 )

Protein structural motif recognition using residual couplings ( 01JACS1222 ).

Changes in ¹⁵N ( 97NAT732 and 00JACS10143 ), ¹³CO ( 98JACS6836 and 00JACS10143 ) and NH ( 00JACS10143 ) chemical shifts in dilute liquid crystalline phases provide information on the magnitude and orientation of the chemical shielding tensors relative to the molecule's alignment frame.

Practical details: ( 98JB361 ).

RDCs in the study of side-chain dynamics:

Measurement of residual ¹H-¹³C and ¹³C-¹³C dipolar couplings of methyl groups ( 99JACS4690 ).

Measurement of residual ¹H-¹³C dipolar couplings of methyl groups ( 01JB77-20 and 02JB35-23) and of beta-CH and beta-CH2 positions ( 01JACS6892 ).

Measurement of residual ¹H-¹³C and ¹H-¹H dipolar couplings in methylene groups ( 00JB99 and 05JB201-31 ).

Xi rotamers can be identified from analysis of several sidechain RDCs ( 01JACS3844 )

Study of the orientation of functional groups in Asn and Gln sidechains ( 01JACS8642 and 01JMR267-153 )

Measurement of ¹J_NH dipolar couplings on paramagnetic proteins to determine the magnetic susceptibility anisotropy.

Dipolar couplings using high-pressure NMR ( 01JB173-21 )

Manipulation of the orientation by variable-angle sample spinning (01JACS910 and 04JB259-29 )

More examples:

02JB169-23

05JB185-31.

Methionine sulfoxide reductase (02JACS13709).

Detecting recognition modes of calmodulin (02BIO12899).