Related ArticlesAn emerging concept of biomolecular dynamics and function: applications of NMR & MRI.
Magn Reson Med Sci. 2002;1(1):27-31
Authors: Kuwata K
A new concept of protein dynamics has emerged quite recently, and a crucial link between protein dynamics and function has been largely established using recent NMR techniques in the solution state. Protein structure is governed by the thermodynamic principle and may not necessarily be unique in the solution state. Enzyme catalysis, protein folding or allosteric transition occurs on the microsecond to millisecond time scale, implying that in order to prepare the specific nuclear coordinate for the electronic state transition, a protein must rearrange its nuclear coordinates substantially, and this process may generally take a long period of time almost comparable to that of protein folding. Protein coordinates optimized for the electronic reaction may form an energy state--which may be called an "excited state"--that is thermodynamically distinct from the native state. In contrast, the native state is called a "ground state." Relevant NMR techniques developed recently may also have useful application to MRI, since the critical time scale of various reactions in a living system is also around micro- to milliseconds.
Compressed sensing and the reconstruction of ultrafast 2D NMR data: Principles and biomolecular applications.
Compressed sensing and the reconstruction of ultrafast 2D NMR data: Principles and biomolecular applications.
Compressed sensing and the reconstruction of ultrafast 2D NMR data: Principles and biomolecular applications.
J Magn Reson. 2011 Apr;209(2):352-8
Authors: Shrot Y, Frydman L
A topic of active investigation in 2D NMR relates to the minimum number of scans required for acquiring this kind of spectra, particularly when these are dictated by sampling rather than by sensitivity considerations. Reductions in this minimum number of scans have...
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07-23-2011 08:54 AM
Methyl groups as probes of supra-molecular structure, dynamics and function
Methyl groups as probes of supra-molecular structure, dynamics and function
Abstract The development of new protein labeling strategies, along with optimized experiments that exploit the label, have significantly impacted on the types of biochemical problems that can now be addressed by solution NMR spectroscopy. Here we describe how methyl labeling of key residues in a highly deuterated protein background has facilitated studies of the structure, dynamics and interactions of supra-molecular particles. The methyl-labeling approach is briefly reviewed, followed by a summary of...
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01-09-2011 12:46 PM
Overcoming the solubility limit with solubility-enhancement tags: successful applications in biomolecular NMR studies
Overcoming the solubility limit with solubility-enhancement tags: successful applications in biomolecular NMR studies
Abstract Although the rapid progress of NMR technology has significantly expanded the range of NMR-trackable systems, preparation of NMR-suitable samples that are highly soluble and stable remains a bottleneck for studies of many biological systems. The application of solubility-enhancement tags (SETs) has been highly effective in overcoming solubility and sample stability issues and has enabled structural studies of important biological systems previously deemed...
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[NMR paper] Structure, dynamics and function of the outer membrane protein A (OmpA) and influenza
Structure, dynamics and function of the outer membrane protein A (OmpA) and influenza hemagglutinin fusion domain in detergent micelles by solution NMR.
Related Articles Structure, dynamics and function of the outer membrane protein A (OmpA) and influenza hemagglutinin fusion domain in detergent micelles by solution NMR.
FEBS Lett. 2003 Nov 27;555(1):139-43
Authors: Tamm LK, Abildgaard F, Arora A, Blad H, Bushweller JH
Recent progress from our laboratories to determine structures of small membrane proteins (up to 20 kDa) in detergent micelles...
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11-24-2010 09:16 PM
[NMR paper] Protein dynamics from solution NMR: theory and applications.
Protein dynamics from solution NMR: theory and applications.
Related Articles Protein dynamics from solution NMR: theory and applications.
Cell Biochem Biophys. 2003;37(3):187-211
Authors: Kempf JG, Loria JP
Solution nuclear magnetic resonance (NMR) spectroscopy is unique in its ability to elucidate the details of atomic-level structural and dynamical properties of biological macromolecules under native-like conditions. Recent advances in NMR techniques and protein sample preparation now allow comprehensive investigation of protein dynamics...
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11-24-2010 09:01 PM
[NMR paper] Correlation of binding-loop internal dynamics with stability and function in potato I
Correlation of binding-loop internal dynamics with stability and function in potato I inhibitor family: relative contributions of Arg(50) and Arg(52) in Cucurbita maxima trypsin inhibitor-V as studied by site-directed mutagenesis and NMR spectroscopy.
Related Articles Correlation of binding-loop internal dynamics with stability and function in potato I inhibitor family: relative contributions of Arg(50) and Arg(52) in Cucurbita maxima trypsin inhibitor-V as studied by site-directed mutagenesis and NMR spectroscopy.
Biochemistry. 2002 Jul 30;41(30):9572-9
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11-24-2010 08:58 PM
[NMR paper] Dynamic activation of protein function: a view emerging from NMR spectroscopy.
Dynamic activation of protein function: a view emerging from NMR spectroscopy.
Related Articles Dynamic activation of protein function: a view emerging from NMR spectroscopy.
Nat Struct Biol. 2001 Nov;8(11):926-31
Authors: Wand AJ
Recent developments in solution NMR methods have allowed for an unprecedented view of protein dynamics. Current insights into the nature of protein dynamics and their potential influence on protein structure, stability and function are reviewed. Particular emphasis is placed on the potential of fast side chain motion...
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11-19-2010 08:44 PM
[NMR paper] Biomolecular solid state NMR: advances in structural methodology and applications to
Biomolecular solid state NMR: advances in structural methodology and applications to peptide and protein fibrils.
Related Articles Biomolecular solid state NMR: advances in structural methodology and applications to peptide and protein fibrils.
Annu Rev Phys Chem. 2001;52:575-606
Authors: Tycko R
Solid state nuclear magnetic resonance (NMR) methods can provide atomic-level structural constraints on peptides and proteins in forms that are not amenable to characterization by other high-resolution structural techniques, owing to insolubility,...