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The electric field effect derives from the polarization of electrons along sigma bonds by the presence of a charged (or partially charged) atom, Thus, an oxygen atom close to the H of a C-H group will push electrons away from the H and so deshield it. This effect is generally assumed simply to be proportional to the strength of the electric field at the proton in the direction of the C-H bond, or: oE = &rEz (2) with E, = C (Q,lr,2)cose (3) Protein Chemical Shifts 55 C X Fig. 1. Definition of terms for the calculation of oE, using an oxygen atom as an example of a source of electric field shift.

Thus, the two experiments are complementary and often are used as a pair. 4. 1. CBCA(CO)NH, CBCANH, HNCACB, HBHA(CBCACO)NH, HBHA(CBCA)NH CBCA(CO)NH (32) (HN, NH, C”pfiI _,) is an extension of HN(CO)CA, as it correlates both the Cs and Ca chemical shifts with the amide from the previous Heteronuclear Assignment Techniques 41 residue. The CBCANH experiment (33) (HN, NH, Ca*sI {CapsI_1}), an extension of HNCA, mainly provides intraresidue connections, but with some interresidue correlations as well.

Since the HNCO essentially is a ‘H--15N HSQC edited by the carbonyi frequency, the overlap was reduced enough for nearly all the resonances to be resolved. 2. These shift pairs were matched to the peaks m the HNCA, TOCSY-HMQC, NOESY-HMQC, HBHA(CO)NH, CBCA(CO)NH, and CBCANH spectra, wtthm a given tolerance for the *HP5N shifts. This gave connectivities between the ‘H/“N amide shifts and the intrarestdue/sequentral Cal Cs, Ha, and Ha shifts. At this stage, however, many of the correlations were not unique.

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