|
|
|
|
| LEADER |
01000naa a22002652 4500 |
| 001 |
NLM18300616X |
| 003 |
DE-627 |
| 005 |
20231223163839.0 |
| 007 |
cr uuu---uuuuu |
| 008 |
231223s2009 xx |||||o 00| ||eng c |
| 024 |
7 |
|
|a 10.1002/mrc.2337
|2 doi
|
| 028 |
5 |
2 |
|a pubmed24n0610.xml
|
| 035 |
|
|
|a (DE-627)NLM18300616X
|
| 035 |
|
|
|a (NLM)18853398
|
| 040 |
|
|
|a DE-627
|b ger
|c DE-627
|e rakwb
|
| 041 |
|
|
|a eng
|
| 100 |
1 |
|
|a Schmidt, Jürgen M
|e verfasserin
|4 aut
|
| 245 |
1 |
0 |
|a Variation in protein C(alpha)-related one-bond J couplings
|
| 264 |
|
1 |
|c 2009
|
| 336 |
|
|
|a Text
|b txt
|2 rdacontent
|
| 337 |
|
|
|a ƒaComputermedien
|b c
|2 rdamedia
|
| 338 |
|
|
|a ƒa Online-Ressource
|b cr
|2 rdacarrier
|
| 500 |
|
|
|a Date Completed 09.02.2009
|
| 500 |
|
|
|a Date Revised 29.01.2022
|
| 500 |
|
|
|a published: Print
|
| 500 |
|
|
|a Citation Status MEDLINE
|
| 520 |
|
|
|a 2008 John Wiley & Sons, Ltd.
|
| 520 |
|
|
|a Four types of polypeptide (1)J(C alpha X) couplings are examined, involving the main-chain carbon C(alpha) and either of four possible substituents. A total 3105 values of (1)J(C alpha H alpha), (1)J(C alpha C beta), (1)J(C alpha C'), and (1)J(C alpha N') were collected from six proteins, averaging 143.4 +/- 3.3, 34.9 +/- 2.5, 52.6 +/- 0.9, and 10.7 +/- 1.2 Hz, respectively. Analysis of variances (ANOVA) reveals a variety of factors impacting on (1)J and ranks their relative statistical significance and importance to biomolecular NMR structure refinement. Accordingly, the spread in the (1)J values is attributed, in equal proportions, to amino-acid specific substituent patterns and to polypeptide-chain geometry, specifically torsions phi, psi, and chi(1) circumjacent to C(alpha). The (1)J coupling constants correlate with protein secondary structure. For alpha-helical phi, psi combinations, (1)J(C alpha H alpha) is elevated by more than one standard deviation (147.8 Hz), while both (1)J(C alpha N') and (1)J(C alpha C beta) fall short of their grand means (9.5 and 33.7 Hz). Rare positive phi torsion angles in proteins exhibit concomitant small (1)J(C alpha H alpha) and (1)J(C alpha N') (138.4 and 9.6 Hz) and large (1)J(C alpha C beta) (39.9 Hz) values. The (1)J(C alpha N') coupling varies monotonously over the phi torsion range typical of beta-sheet secondary structure and is largest (13.3 Hz) for phi around -160 degrees. All four coupling types depend on psi and thus help determine a torsion that is notoriously difficult to assess by traditional approaches using (3)J. Influences on (1)J stemming from protein secondary structure and other factors, such as amino-acid composition, are largely independent
|
| 650 |
|
4 |
|a Journal Article
|
| 650 |
|
4 |
|a Research Support, Non-U.S. Gov't
|
| 650 |
|
7 |
|a Proteins
|2 NLM
|
| 700 |
1 |
|
|a Howard, Mark J
|e verfasserin
|4 aut
|
| 700 |
1 |
|
|a Maestre-Martínez, Mitcheell
|e verfasserin
|4 aut
|
| 700 |
1 |
|
|a Pérez, Carlos S
|e verfasserin
|4 aut
|
| 700 |
1 |
|
|a Löhr, Frank
|e verfasserin
|4 aut
|
| 773 |
0 |
8 |
|i Enthalten in
|t Magnetic resonance in chemistry : MRC
|d 1985
|g 47(2009), 1 vom: 04. Jan., Seite 16-30
|w (DE-627)NLM098179667
|x 1097-458X
|7 nnns
|
| 773 |
1 |
8 |
|g volume:47
|g year:2009
|g number:1
|g day:04
|g month:01
|g pages:16-30
|
| 856 |
4 |
0 |
|u http://dx.doi.org/10.1002/mrc.2337
|3 Volltext
|
| 912 |
|
|
|a GBV_USEFLAG_A
|
| 912 |
|
|
|a SYSFLAG_A
|
| 912 |
|
|
|a GBV_NLM
|
| 912 |
|
|
|a GBV_ILN_350
|
| 951 |
|
|
|a AR
|
| 952 |
|
|
|d 47
|j 2009
|e 1
|b 04
|c 01
|h 16-30
|