Orienting molecular fragments and molecules with residual dipolar couplings

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Orienting molecular fragments and molecules with residual dipolar couplings. / Skrynnikov, Nikolai R.

In: Comptes Rendus Physique, Vol. 5, No. 3, 04.2004, p. 359-375.

Research output: Contribution to journal › Short survey › peer-review

Author

Skrynnikov, Nikolai R. / Orienting molecular fragments and molecules with residual dipolar couplings. In: Comptes Rendus Physique. 2004 ; Vol. 5, No. 3. pp. 359-375.

BibTeX

@article{96a943c738a747868046fab28fe934ce,

title = "Orienting molecular fragments and molecules with residual dipolar couplings",

abstract = "Many proteins and nucleic acids, as well as their complexes, consist of structural units with a known internal structure. However, relative position of these units within the entity is often a subject of uncertainty. This problem can be effectively addressed with the help of residual dipolar couplings (RDCs) measured by solution-state NMR in weakly oriented samples. Using a rigid-body approach, the relative orientation of the structural units can be adjusted to match the experimental RDC data. This paper explains why the rigid-body approach is well suited for application with the RDC data and discusses the general algorithm suitable for such studies. The examples of RDC-based rigid-body treatment involving protein backbone fragments, RNA helices, multidomain proteins, protein-ligand systems, and protein complexes are described in detail. The discussion includes systems where multiple structures co-exist in a dynamic equilibrium. Various degeneracies associated with the RDC data are considered and the methods that can assist in resolving the ambiguities are described.",

keywords = "Residual dipolar couplings, Solution-state NMR",

author = "Skrynnikov, {Nikolai R.}",

year = "2004",

month = apr,

doi = "10.1016/j.crhy.2004.02.006",

language = "English",

volume = "5",

pages = "359--375",

journal = "Comptes Rendus Physique",

issn = "1631-0705",

publisher = "Elsevier",

number = "3",

}

RIS

TY - JOUR

T1 - Orienting molecular fragments and molecules with residual dipolar couplings

AU - Skrynnikov, Nikolai R.

PY - 2004/4

Y1 - 2004/4

N2 - Many proteins and nucleic acids, as well as their complexes, consist of structural units with a known internal structure. However, relative position of these units within the entity is often a subject of uncertainty. This problem can be effectively addressed with the help of residual dipolar couplings (RDCs) measured by solution-state NMR in weakly oriented samples. Using a rigid-body approach, the relative orientation of the structural units can be adjusted to match the experimental RDC data. This paper explains why the rigid-body approach is well suited for application with the RDC data and discusses the general algorithm suitable for such studies. The examples of RDC-based rigid-body treatment involving protein backbone fragments, RNA helices, multidomain proteins, protein-ligand systems, and protein complexes are described in detail. The discussion includes systems where multiple structures co-exist in a dynamic equilibrium. Various degeneracies associated with the RDC data are considered and the methods that can assist in resolving the ambiguities are described.

AB - Many proteins and nucleic acids, as well as their complexes, consist of structural units with a known internal structure. However, relative position of these units within the entity is often a subject of uncertainty. This problem can be effectively addressed with the help of residual dipolar couplings (RDCs) measured by solution-state NMR in weakly oriented samples. Using a rigid-body approach, the relative orientation of the structural units can be adjusted to match the experimental RDC data. This paper explains why the rigid-body approach is well suited for application with the RDC data and discusses the general algorithm suitable for such studies. The examples of RDC-based rigid-body treatment involving protein backbone fragments, RNA helices, multidomain proteins, protein-ligand systems, and protein complexes are described in detail. The discussion includes systems where multiple structures co-exist in a dynamic equilibrium. Various degeneracies associated with the RDC data are considered and the methods that can assist in resolving the ambiguities are described.

KW - Residual dipolar couplings

KW - Solution-state NMR

UR - http://www.scopus.com/inward/record.url?scp=2442452778&partnerID=8YFLogxK

U2 - 10.1016/j.crhy.2004.02.006

DO - 10.1016/j.crhy.2004.02.006

M3 - Short survey

AN - SCOPUS:2442452778

VL - 5

SP - 359

EP - 375

JO - Comptes Rendus Physique

JF - Comptes Rendus Physique

SN - 1631-0705

IS - 3

ER -

ID: 87882697