TY - JOUR
T1 - Isotope-labeling strategies for solution NMR studies of macromolecular assemblies
AU - Zhang, Heyi
AU - van Ingen, Hugo
PY - 2016/6/1
Y1 - 2016/6/1
N2 - Proteins come together in macromolecular assemblies, recognizing and binding to each other through their structures, and operating on their substrates through their motions. Detailed characterization of these processes is particularly suited to NMR, a high-resolution technique sensitive to structure, dynamics, and interactions. Advances in isotope-labeling have enabled such studies to an ever-increasing range of systems. Here we highlight recent applications and bring to the fore the range of options to produce labeled proteins and to control the specific placement of isotopes. The increased labeling control and affordability, together with the possibility to combine strategies will further deepen and extend the range of protein assembly investigations.
AB - Proteins come together in macromolecular assemblies, recognizing and binding to each other through their structures, and operating on their substrates through their motions. Detailed characterization of these processes is particularly suited to NMR, a high-resolution technique sensitive to structure, dynamics, and interactions. Advances in isotope-labeling have enabled such studies to an ever-increasing range of systems. Here we highlight recent applications and bring to the fore the range of options to produce labeled proteins and to control the specific placement of isotopes. The increased labeling control and affordability, together with the possibility to combine strategies will further deepen and extend the range of protein assembly investigations.
UR - http://www.scopus.com/inward/record.url?scp=84973440928&partnerID=8YFLogxK
U2 - 10.1016/j.sbi.2016.05.008
DO - 10.1016/j.sbi.2016.05.008
M3 - Review article
AN - SCOPUS:84973440928
SN - 0959-440X
VL - 38
SP - 75
EP - 82
JO - Current Opinion in Structural Biology
JF - Current Opinion in Structural Biology
ER -