Solid-state N
MR can provide ato
mic-resolution infor
mation about protein
motions occurring on a vast range of ti
me scales under si
milar conditions to those of X-ray diffraction studies and therefore offers a highly co
mple
mentary approach to characterizing the dyna
mic fluctuations occurring in the crystal. We co
mpare experi
mentally deter
mined dyna
mic para
meters, spin relaxation, che
mical shifts, and dipolar couplings, to values calculated fro
m a 200 ns MD si
mulation of protein GB1 in its crystalline for
m, providing insight into the nature of structural dyna
mics occurring within the crystalline lattice. This si
mulation allows us to test the accuracy of co
mmonly applied procedures for the interpretation of experi
mental solid-state relaxation data in ter
ms of dyna
mic
modes and ti
me scales. We discover that the potential co
mplexity of relaxation-active
motion can lead to significant under- or overesti
mation of dyna
mic a
mplitudes if different co
mponents are not taken into consideration.
Keywords:
mics&qsSearchArea=searchText">protein dynamics; NMR; crystalline protein; molecular+dynamics&qsSearchArea=searchText">molecular dynamics; mational+dynamics&qsSearchArea=searchText">conformational dynamics