15N NMR Relaxation Data Reveal Significant Chemical Exchange Broadening in the α-Domain of Human α-Lactalbumin

Biochemistry ◽  
2009 ◽  
Vol 48 (19) ◽  
pp. 4031-4039 ◽  
Author(s):  
Gilles Bruylants ◽  
Christina Redfield
Keyword(s):  
Chemical Exchange ◽  
Nmr Relaxation ◽  
15N Nmr ◽  
Relaxation Data ◽  
15N Nmr Relaxation ◽  
Significant Chemical ◽  
Exchange Broadening

A suite of Mathematica notebooks for the analysis of protein main chain 15N NMR relaxation data

2006 ◽  
Vol 36 (4) ◽  
pp. 215-224 ◽  
Author(s):  
Leo Spyracopoulos
Keyword(s):  
Main Chain ◽  
Nmr Relaxation ◽  
15N Nmr ◽  
Relaxation Data ◽  
15N Nmr Relaxation

Analysis of the backbone dynamics of capsicein using 15N NMR relaxation rate measurements

1994 ◽  
Vol 91 ◽  
pp. 776-784
Author(s):  
C van Heijenoort ◽  
S Bouaziz ◽  
E Guittet
Keyword(s):  
Relaxation Rate ◽  
Nmr Relaxation ◽  
Backbone Dynamics ◽  
15N Nmr ◽  
15N Nmr Relaxation

Detection of Chemical Exchange in Methyl Groups of Macromolecules

2019 ◽  
Author(s):  
Michelle Gill ◽  
Andrew Hsu ◽  
Arthur G. Palmer, III
Keyword(s):  
Relaxation Rate ◽  
Chemical Exchange ◽  
Double Quantum ◽  
Methyl Groups ◽  
Multiple Quantum ◽  
Relaxation Data ◽  
E Coli ◽  
Methyl Trosy ◽  
Dynamics Simulations ◽  
Exchange Broadening

<div> <div> <div> <p>The zero- and double-quantum methyl TROSY Hahn-echo and the methyl <sup>1</sup>H-<sup>1</sup>H dipole- dipole cross-correlation nuclear magnetic resonance experiments enable estimation of multiple quantum chemical exchange broadening in methyl groups in proteins. The two relaxation rate constants are established to be linearly dependent using molecular dynamics simulations and empirical analysis of experimental data. This relationship allows chemical exchange broadening to be recognized as an increase in the Hahn-echo relaxation rate constant. The approach is illustrated by analyzing relaxation data collected at three temperatures for <i>E. coli </i>ribonuclease HI and by analyzing relaxation data collected for different cofactor and substrate complexes of <i>E. coli </i>AlkB. </p> </div> </div> </div>

Backbone dynamics of the CDK inhibitor p19INK4d studied by 15N NMR relaxation experiments at two field strengths

1998 ◽  
Vol 283 (1) ◽  
pp. 221-229 ◽  
Author(s):  
Christian Renner ◽  
Roland Baumgartner ◽  
Angelika A Noegel ◽  
Tad A Holak
Keyword(s):  
Nmr Relaxation ◽  
Backbone Dynamics ◽  
15N Nmr ◽  
Cdk Inhibitor ◽  
15N Nmr Relaxation ◽  
Relaxation Experiments ◽  
Field Strengths

scholarly journals Analysis of Backbone Dynamics in Cytochrome b5 using 15N-NMR Relaxation Measurements

1997 ◽  
Vol 245 (2) ◽  
pp. 349-354 ◽  
Author(s):  
Geoffrey P. Kelly ◽  
Frederick W. Muskett ◽  
David Whitford
Keyword(s):  
Cytochrome B5 ◽  
Nmr Relaxation ◽  
Backbone Dynamics ◽  
15N Nmr ◽  
15N Nmr Relaxation ◽  
Relaxation Measurements

scholarly journals Mobility of Histidine Side Chains Analyzed with 15N NMR Relaxation and Cross-Correlation Data: Insight into Zinc-Finger–DNA Interactions

2019 ◽  
Vol 123 (17) ◽  
pp. 3706-3710
Author(s):  
Catherine A. Kemme ◽  
Ross H. Luu ◽  
Chuanying Chen ◽  
Channing C. Pletka ◽  
B. Montgomery Pettitt ◽  
...  
Keyword(s):  
Zinc Finger ◽  
Cross Correlation ◽  
Nmr Relaxation ◽  
15N Nmr ◽  
Side Chains ◽  
Dna Interactions ◽  
15N Nmr Relaxation ◽  
Correlation Data ◽  
Insight Into

Analysis of Internal Motions of RNase T1 Complexed with a Productive Substrate Involving 15N NMR Relaxation Measurements

2006 ◽  
Vol 140 (1) ◽  
pp. 43-48
Author(s):  
Yuichiro Yoshida ◽  
Masakazu Tanaka ◽  
Takatoshi Ohkuri ◽  
Yoshitsugu Tanaka ◽  
Taiji Imoto ◽  
...  
Keyword(s):  
Nmr Relaxation ◽  
15N Nmr ◽  
Internal Motions ◽  
15N Nmr Relaxation ◽  
Relaxation Measurements

Triple resonance 15N NMR relaxation experiments for studies of intrinsically disordered proteins

2017 ◽  
Vol 69 (3) ◽  
pp. 133-146 ◽  
Author(s):  
Pavel Srb ◽  
Jiří Nováček ◽  
Pavel Kadeřávek ◽  
Alžbeta Rabatinová ◽  
Libor Krásný ◽  
...  
Keyword(s):  
Intrinsically Disordered Proteins ◽  
Nmr Relaxation ◽  
Disordered Proteins ◽  
15N Nmr ◽  
Triple Resonance ◽  
Intrinsically Disordered ◽  
15N Nmr Relaxation ◽  
Relaxation Experiments

scholarly journals Detection of Chemical Exchange in Methyl Groups of Macromolecules

2019 ◽  
Author(s):  
Michelle Gill ◽  
Andrew Hsu ◽  
Arthur G. Palmer, III
Keyword(s):  
Relaxation Rate ◽  
Chemical Exchange ◽  
Double Quantum ◽  
Methyl Groups ◽  
Multiple Quantum ◽  
Relaxation Data ◽  
E Coli ◽  
Methyl Trosy ◽  
Dynamics Simulations ◽  
Exchange Broadening

<div> <div> <div> <p>The zero- and double-quantum methyl TROSY Hahn-echo and the methyl <sup>1</sup>H-<sup>1</sup>H dipole- dipole cross-correlation nuclear magnetic resonance experiments enable estimation of multiple quantum chemical exchange broadening in methyl groups in proteins. The two relaxation rate constants are established to be linearly dependent using molecular dynamics simulations and empirical analysis of experimental data. This relationship allows chemical exchange broadening to be recognized as an increase in the Hahn-echo relaxation rate constant. The approach is illustrated by analyzing relaxation data collected at three temperatures for <i>E. coli </i>ribonuclease HI and by analyzing relaxation data collected for different cofactor and substrate complexes of <i>E. coli </i>AlkB. </p> </div> </div> </div>

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