1999
DOI: 10.1021/bi9905213
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Domain Orientation and Dynamics in Multidomain Proteins from Residual Dipolar Couplings

Abstract: The data most commonly available for the determination of macromolecular structures in solution are NOE based distance estimates and spin-spin coupling constant based dihedral angle estimates. This information is, unfortunately, inherently short-range in nature. Thus, for many multidomain proteins, little information is available to accurately position weakly interacting domains with respect to each other. Recent studies of proteins aligned in dilute liquid crystalline solvents have shown the utility of measur… Show more

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Cited by 259 publications
(269 citation statements)
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“…For hetero-oligomeric complexes, of course, one can determine alignment tensors independently for each subunit and assemble a structure by rotating subunits to superimpose principal axis systems. 9,10,13,14,38 One of the primary limitations of the methods described is that the structure of the monomeric unit must be available. This structure could come from existing crystal structures that may not show the proper assembly for weak complexes, or it could come from NMR based structure determination.…”
Section: Discussionmentioning
confidence: 99%
“…For hetero-oligomeric complexes, of course, one can determine alignment tensors independently for each subunit and assemble a structure by rotating subunits to superimpose principal axis systems. 9,10,13,14,38 One of the primary limitations of the methods described is that the structure of the monomeric unit must be available. This structure could come from existing crystal structures that may not show the proper assembly for weak complexes, or it could come from NMR based structure determination.…”
Section: Discussionmentioning
confidence: 99%
“…Following the derivation by Favro 33 , we write (7) where a r , m are decomposition coefficients and E r are the corresponding rate constants which depend solely on the principal values {D x , D y , D z } of the rotational diffusion tensor D (see Supporting Information).…”
Section: The Overall Tumbling Modementioning
confidence: 99%
“…Weak alignment of proteins, which can exist naturally due to the paramagnetic properties of the molecule (Tolman et al, 1995) or be induced by solvation in liquid crystal media (Tjandra & Bax, 1997), lipid bicelles (Sanders et al, 1994) or a suspension of ®la-mentous bacteriophage (Hansen et al, 1998), prevents complete averaging of the dipolar interaction while retaining the solution properties necessary for high resolution NMR. The measurement of dipolar couplings under these conditions provides long-range order constraints which, in combination with classical NOE data, have been shown to improve structure determination in multidomain systems and protein-ligand complexes (Tjandra, 1999;Fischer et al, 1999;Olejniczak et al, 1999;Clore & Garrett et al, 1999;Bolon et al, 1999). Nevertheless, the determination of three-dimensional protein structure using only orientational information is severely hindered by the lack of long-range distances that de®ne the topology of the molecule.…”
Section: Introductionmentioning
confidence: 99%