2000
DOI: 10.1017/s0033583500003656
|View full text |Cite
|
Sign up to set email alerts
|

Abstract: 1. Introduction 3721.1 Residual dipolar couplings as a route to structure and dynamics 3721.2 A brief history of oriented phase high resolution NMR 3742. Theoretical treatment of dipolar interactions 3762.1 Anisotropic interactions as probes of macromolecular structure and dynamics 3762.1.1 The dipolar interaction 3762.1.2 Averaging in the solution state 3772.2 Ordering of a rigid body 3772.2.1 The Saupe order tensor 3782.2.2 Orientational probability distribution function 3802.2.3 The generalized degree of or… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
1
1
1

Citation Types

5
413
0
10

Year Published

2002
2002
2016
2016

Publication Types

Select...
6
3

Relationship

0
9

Authors

Journals

citations
Cited by 417 publications
(428 citation statements)
references
References 123 publications
5
413
0
10
Order By: Relevance
“…Ramachandran analysis was used to confirm the good quality of the structure. Of the residues, 81.4% have backbone conformation in the most favored regions, and most residues in less favorable conformations are from the poorly defined region (27)(28)(29)(30)(31)(32)(33)(34)(35).…”
Section: Structure Determinationmentioning
confidence: 99%
“…Ramachandran analysis was used to confirm the good quality of the structure. Of the residues, 81.4% have backbone conformation in the most favored regions, and most residues in less favorable conformations are from the poorly defined region (27)(28)(29)(30)(31)(32)(33)(34)(35).…”
Section: Structure Determinationmentioning
confidence: 99%
“…Slow time scales are, however, of particular interest because functionally important biological processes, including enzyme catalysis (11), signal transduction (12), ligand binding, and allosteric regulation (13), as well as collective motions involving groups of atoms or whole amino acids (14), are expected to occur in this time range. Residual dipolar couplings (RDCs) report on averages over longer time scales (up to the millisecond range) and therefore encode key information for understanding slower protein motions over a very broad time scale (15,16). Recent studies have exploited the orientational averaging properties of RDCs to characterize the amplitude and direction of motions of NH vectors (17)(18)(19) or to study local variations in position and dynamics of the amide proton (20,21).…”
mentioning
confidence: 99%
“…It is now well established that RDCs can provide direct information on the preferred orientations of various structural elements in proteins [see reviews, (27) and (28)]. However, obtaining data under conditions where small environment-induced changes are of interest is challenging.…”
mentioning
confidence: 99%