NMR approaches for structural analysis of multidomain proteins and complexes in solution
NMR spectroscopy is a key method for studying the structure and dynamics of (large)
multidomain proteins and complexes in solution. It plays a unique role in integrated …
multidomain proteins and complexes in solution. It plays a unique role in integrated …
NMR studies of dynamic biomolecular conformational ensembles
DA Torchia - Progress in nuclear magnetic resonance spectroscopy, 2015 - Elsevier
Multidimensional heteronuclear NMR approaches can provide nearly complete sequential
signal assignments of isotopically enriched biomolecules. The availability of assignments …
signal assignments of isotopically enriched biomolecules. The availability of assignments …
Interdomain dynamics explored by paramagnetic NMR
L Russo, M Maestre-Martinez, S Wolff… - Journal of the …, 2013 - ACS Publications
An ensemble-based approach is presented to explore the conformational space sampled by
a multidomain protein showing moderate interdomain dynamics in terms of translational and …
a multidomain protein showing moderate interdomain dynamics in terms of translational and …
Examination of matrix metalloproteinase-1 in solution: a preference for the pre-collagenolysis state
Catalysis of collagen degradation by matrix metalloproteinase 1 (MMP-1) has been
proposed to critically rely on flexibility between the catalytic (CAT) and hemopexin-like …
proposed to critically rely on flexibility between the catalytic (CAT) and hemopexin-like …
Protein assembly and building blocks: beyond the limits of the LEGO brick metaphor
Y Levy - Biochemistry, 2017 - ACS Publications
Proteins, like other biomolecules, have a modular and hierarchical structure. Various
building blocks are used to construct proteins of high structural complexity and diverse …
building blocks are used to construct proteins of high structural complexity and diverse …
Insights into domain–domain motions in proteins and RNA from solution NMR
Conspectus Many multidomain proteins and ribonucleic acids consist of domains that
autonomously fold and that are linked together by flexible junctions. This architectural …
autonomously fold and that are linked together by flexible junctions. This architectural …
Folding of multidomain proteins: Biophysical consequences of tethering even in apparently independent folding
O Arviv, Y Levy - Proteins: Structure, Function, and …, 2012 - Wiley Online Library
Most eukaryotic and a substantial fraction of prokaryotic proteins are composed of more than
one domain. The tethering of these evolutionary, structural, and functional units raises …
one domain. The tethering of these evolutionary, structural, and functional units raises …
Investigating protein conformational energy landscapes and atomic resolution dynamics from NMR dipolar couplings: a review
L Salmon, M Blackledge - Reports on Progress in Physics, 2015 - iopscience.iop.org
Nuclear magnetic resonance spectroscopy is exquisitely sensitive to protein dynamics. In
particular inter-nuclear dipolar couplings, that become measurable in solution when the …
particular inter-nuclear dipolar couplings, that become measurable in solution when the …
Determination of the Individual Roles of the Linker Residues in the Inter-Domain Motions of Calmodulin using NMR Chemical Shifts
Many protein molecules are formed by two or more domains whose structures and dynamics
are closely related to their biological functions. It is challenging, however, to determine the …
are closely related to their biological functions. It is challenging, however, to determine the …
Model of a six immunoglobulin-like domain fragment of filamin A (16–21) built using residual dipolar couplings
H Tossavainen, O Koskela, P Jiang… - Journal of the …, 2012 - ACS Publications
Filamins are actin-binding proteins that participate in a wide range of cell functions,
including cell morphology, locomotion, membrane protein localization, and intracellular …
including cell morphology, locomotion, membrane protein localization, and intracellular …