Internal Consistency of NMR Data Obtained in Partially Aligned
Biomacromolecules

J 2003

Internal Consistency of NMR Data Obtained in Partially Aligned Biomacromolecules

ŽÍDEK, Lukáš, Petr PADRTA, Josef CHMELÍK a Vladimír SKLENÁŘ

Základní údaje

Originální název

Internal Consistency of NMR Data Obtained in Partially Aligned Biomacromolecules

Autoři

ŽÍDEK, Lukáš (203 Česká republika), Petr PADRTA (203 Česká republika), Josef CHMELÍK (203 Česká republika) a Vladimír SKLENÁŘ (203 Česká republika, garant)

Vydání

Journal of Magnetic Resonance, San Diego, Academic Press, 2003, 1090-7807

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10600 1.6 Biological sciences

Stát vydavatele

Spojené státy

Utajení

není předmětem státního či obchodního tajemství

Impakt faktor

Impact factor: 2.084

Kód RIV

RIV/00216224:14310/03:00008778

Organizační jednotka

Přírodovědecká fakulta

UT WoS

000183923800018

Klíčová slova anglicky

residual dipolar couplings; chemical shift anisotropy; peptide plane; nucleic acids base

Štítky

chemical shift anisotropy, nucleic acids base, peptide plane, residual dipolar couplings

Změněno: 20. 6. 2008 12:55, prof. RNDr. Vladimír Sklenář, DrSc.

Anotace

V originále

A method of testing structure-related NMR data prior to structure calculations is presented. The test is applicable to second rank tensor interactions (dipolar coupling, anisotropic chemical shielding, quadrupolar interaction) observed in partially aligned samples of biomacromolecules. The method utilizes the fact that only limited number of frequencies corresponding to the mentioned interactions may be measured independently in a rigid fragment of the macromolecule. Additional values can be predicted as linear combinations of the set of independent frequencies. Internal consistency of sufficiently large sets of frequencies measured in individual molecular fragments is tested by comparing the experimental data with their predicted values. The method requires only knowledge of local geometry (i.e., definition of the interaction tensors in the local coordinate frames of the fragments). No information about the alignment or shape of the molecule is required. The test is best suited for planar fragments. Application to peptide bonds and nucleic acid bases is demonstrated.

Návaznosti

LN00A016, projekt VaV

Název: BIOMOLEKULÁRNÍ CENTRUM

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, Biomolekulární centrum

Citovat

ŽÍDEK, Lukáš, Petr PADRTA, Josef CHMELÍK a Vladimír SKLENÁŘ. Internal Consistency of NMR Data Obtained in Partially Aligned Biomacromolecules. Journal of Magnetic Resonance. San Diego: Academic Press, 2003, roč. 162, č. 1, s. 385-395. ISSN 1090-7807.

@article{487506,
   author = {Žídek, Lukáš and Padrta, Petr and Chmelík, Josef and Sklenář, Vladimír},
   article_location = {San Diego},
   article_number = {1},
   keywords = {residual dipolar couplings; chemical shift anisotropy; peptide plane; nucleic acids base},
   language = {eng},
   issn = {1090-7807},
   journal = {Journal of Magnetic Resonance},
   title = {Internal Consistency of NMR Data Obtained in Partially Aligned Biomacromolecules},
   volume = {162},
   year = {2003}
}

TY  - JOUR
ID  - 487506
AU  - Žídek, Lukáš - Padrta, Petr - Chmelík, Josef - Sklenář, Vladimír
PY  - 2003
TI  - Internal Consistency of NMR Data Obtained in Partially Aligned Biomacromolecules
JF  - Journal of Magnetic Resonance
VL  - 162
IS  - 1
SP  - 385-395
EP  - 385-395
PB  - Academic Press
SN  - 10907807
KW  - residual dipolar couplings
KW  - chemical shift anisotropy
KW  - peptide plane
KW  - nucleic acids base
N2  - A method of testing structure-related NMR data prior to structure calculations is presented. The test is applicable to second rank tensor interactions (dipolar coupling, anisotropic chemical shielding, quadrupolar interaction) observed in partially aligned samples of biomacromolecules. The method utilizes the fact that only limited number of frequencies corresponding to the mentioned interactions may be measured independently in a rigid fragment of the macromolecule. Additional values can be predicted as linear combinations of the set of independent frequencies. Internal consistency of sufficiently large sets of frequencies measured in individual molecular fragments is tested by comparing the experimental data with their predicted values. The method requires only knowledge of local geometry (i.e., definition of the interaction tensors in the local coordinate frames of the fragments). No information about the alignment or shape of the molecule is required. The test is best suited for planar fragments. Application to peptide bonds and nucleic acid bases is demonstrated.
ER  -

ŽÍDEK, Lukáš, Petr PADRTA, Josef CHMELÍK a Vladimír SKLENÁŘ. Internal Consistency of NMR Data Obtained in Partially Aligned Biomacromolecules. \textit{Journal of Magnetic Resonance}. San Diego: Academic Press, 2003, roč.~162, č.~1, s.~385-395. ISSN~1090-7807.

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