Literature DB >> 22910879

Application of the quasi-spectral density function of (15)N nuclei to the selection of a motional model for model-free analysis.

R Ishima1, K Yamasaki, K Nagayama.   

Abstract

Parameters used in model-free analysis were related to simulated spectral density functions in a frequency region experimentally obtained by quasi-spectral density function analysis of (15)N nuclei. Five kinds of motional models used in recent model-free analyses were characterized by a simple classification of the experimental spectral density function. We demonstrate advantages and limitations of each of the motional models. To verify the character of the models, model selection using experimental spectral density functions was examined.

Year:  1995        PMID: 22910879     DOI: 10.1007/BF00197640

Source DB:  PubMed          Journal:  J Biomol NMR        ISSN: 0925-2738            Impact factor:   2.835


  13 in total

1.  Analysis of the backbone dynamics of the ribonuclease H domain of the human immunodeficiency virus reverse transcriptase using 15N relaxation measurements.

Authors:  R Powers; G M Clore; S J Stahl; P T Wingfield; A Gronenborn
Journal:  Biochemistry       Date:  1992-09-29       Impact factor: 3.162

2.  Comparison of the backbone dynamics of a folded and an unfolded SH3 domain existing in equilibrium in aqueous buffer.

Authors:  N A Farrow; O Zhang; J D Forman-Kay; L E Kay
Journal:  Biochemistry       Date:  1995-01-24       Impact factor: 3.162

3.  Characterization of the internal motions of Escherichia coli ribonuclease HI by a combination of 15N-NMR relaxation analysis and molecular dynamics simulation: examination of dynamic models.

Authors:  K Yamasaki; M Saito; M Oobatake; S Kanaya
Journal:  Biochemistry       Date:  1995-05-23       Impact factor: 3.162

4.  Mapping of the spectral densities of N-H bond motions in eglin c using heteronuclear relaxation experiments.

Authors:  J W Peng; G Wagner
Journal:  Biochemistry       Date:  1992-09-15       Impact factor: 3.162

5.  Backbone dynamics of proteins as studied by 15N inverse detected heteronuclear NMR spectroscopy: application to staphylococcal nuclease.

Authors:  L E Kay; D A Torchia; A Bax
Journal:  Biochemistry       Date:  1989-11-14       Impact factor: 3.162

6.  Rotational dynamics of calcium-free calmodulin studied by 15N-NMR relaxation measurements.

Authors:  N Tjandra; H Kuboniwa; H Ren; A Bax
Journal:  Eur J Biochem       Date:  1995-06-15

7.  15N NMR relaxation studies of the FK506 binding protein: dynamic effects of ligand binding and implications for calcineurin recognition.

Authors:  J W Cheng; C A Lepre; J M Moore
Journal:  Biochemistry       Date:  1994-04-12       Impact factor: 3.162

8.  Backbone dynamics of a free and phosphopeptide-complexed Src homology 2 domain studied by 15N NMR relaxation.

Authors:  N A Farrow; R Muhandiram; A U Singer; S M Pascal; C M Kay; G Gish; S E Shoelson; T Pawson; J D Forman-Kay; L E Kay
Journal:  Biochemistry       Date:  1994-05-17       Impact factor: 3.162

9.  Backbone dynamics of the Bacillus subtilis glucose permease IIA domain determined from 15N NMR relaxation measurements.

Authors:  M J Stone; W J Fairbrother; A G Palmer; J Reizer; M H Saier; P E Wright
Journal:  Biochemistry       Date:  1992-05-12       Impact factor: 3.162

10.  Protein backbone dynamics revealed by quasi spectral density function analysis of amide N-15 nuclei.

Authors:  R Ishima; K Nagayama
Journal:  Biochemistry       Date:  1995-03-14       Impact factor: 3.162

View more
  5 in total

1.  Lipari-Szabo mapping: A graphical approach to Lipari-Szabo analysis of NMR relaxation data using reduced spectral density mapping.

Authors:  M Andrec; G T Montelione; R M Levy
Journal:  J Biomol NMR       Date:  2000-10       Impact factor: 2.835

2.  Detection of nano-second internal motion and determination of overall tumbling times independent of the time scale of internal motion in proteins from NMR relaxation data.

Authors:  Göran Larsson; Gary Martinez; Jürgen Schleucher; Sybren S Wijmenga
Journal:  J Biomol NMR       Date:  2003-12       Impact factor: 2.835

3.  Assessing the native state conformational distribution of ubiquitin by peptide acidity.

Authors:  Griselda Hernández; Janet S Anderson; David M LeMaster
Journal:  Biophys Chem       Date:  2010-10-15       Impact factor: 2.352

4.  Comparison of 15N- and 13C-determined parameters of mobility in melittin.

Authors:  L Zhu; F G Prendergast; M D Kemple
Journal:  J Biomol NMR       Date:  1998-07       Impact factor: 2.835

Review 5.  NMR Provides Unique Insight into the Functional Dynamics and Interactions of Intrinsically Disordered Proteins.

Authors:  Aldo R Camacho-Zarco; Vincent Schnapka; Serafima Guseva; Anton Abyzov; Wiktor Adamski; Sigrid Milles; Malene Ringkjøbing Jensen; Lukas Zidek; Nicola Salvi; Martin Blackledge
Journal:  Chem Rev       Date:  2022-04-21       Impact factor: 72.087

  5 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.