Protein complexes studied by NMR spectroscopy. Academic Article

abstract

• Recent advances in NMR methods now allow protein complexes to be studied in great detail in a wide range of solution conditions. Isotope-enrichment strategies, resonance-assignment approaches and structural-determination methods have evolved to the point where almost any type of complex involving proteins of reasonable size may be studied in a straightforward way. A variety of isotope editing and filtering strategies underlie these powerful methodologies. Approaches to the characterization of the dynamics of protein complexes have also matured to the point where detailed studies of the effects of complexation on dynamics can be studied over a wide range of timescales.

authors

• Wand, Joshua

published proceedings

• Curr Opin Biotechnol

altmetric score

• 6

author list (cited authors)

• Wand, A. J., & Englander, S. W.

citation count

• 32

complete list of authors

• Wand, AJ||Englander, SW

publication date

• August 1996

publisher

• Elsevier  Publisher

published in

• Current Opinion in Biotechnology  Journal

keywords

• Ligands
• Magnetic Resonance Spectroscopy
• Nucleic Acids
• Protein Conformation
• Proteins

PubMed Central ID

• 8768898

Digital Object Identifier (DOI)

• 10.1016/s0958-1669(96)80115-7

start page

• 403

end page

• 408

volume

• 7

issue

• 4

URL

• http://dx.doi.org/10.1016/s0958-1669(96)80115-7