Heteronuclear Adiabatic Relaxation Dispersion (HARD) for quantitative analysis of conformational dynamics in proteins.
about
Chemical exchange in biomacromolecules: past, present, and future.Measuring dynamic and kinetic information in the previously inaccessible supra-τ(c) window of nanoseconds to microseconds by solution NMR spectroscopy.General expressions for R1ρ relaxation for N-site chemical exchange and the special case of linear chains.Evaluating the influence of initial magnetization conditions on extracted exchange parameters in NMR relaxation experiments: applications to CPMG and CEST.
P2860
Heteronuclear Adiabatic Relaxation Dispersion (HARD) for quantitative analysis of conformational dynamics in proteins.
description
2012 nî lūn-bûn
@nan
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
2012年论文
@zh
2012年论文
@zh-cn
name
Heteronuclear Adiabatic Relaxa ...... mational dynamics in proteins.
@ast
Heteronuclear Adiabatic Relaxa ...... mational dynamics in proteins.
@en
type
label
Heteronuclear Adiabatic Relaxa ...... mational dynamics in proteins.
@ast
Heteronuclear Adiabatic Relaxa ...... mational dynamics in proteins.
@en
prefLabel
Heteronuclear Adiabatic Relaxa ...... mational dynamics in proteins.
@ast
Heteronuclear Adiabatic Relaxa ...... mational dynamics in proteins.
@en
P2093
P2860
P1476
Heteronuclear Adiabatic Relaxa ...... rmational dynamics in proteins
@en
P2093
Burckhard Seelig
Gianluigi Veglia
Larry R Masterson
Michael Garwood
Nathaniel J Traaseth
Shalom Michaeli
P2860
P356
10.1016/J.JMR.2012.03.024
P577
2012-04-06T00:00:00Z