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The Quiet Renaissance of Protein Nuclear Magnetic Resonance

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TLDR
Recent advances in protein NMR that herald a renaissance in which a number of its most important applications reflect the broad problem-solving capability displayed by this method during its classical era during the 1970s and early 1980s are surveyed.
Abstract
From roughly 1985 through the start of the new millennium, the cutting edge of solution protein nuclear magnetic resonance (NMR) spectroscopy was to a significant extent driven by the aspiration to determine structures. Here we survey recent advances in protein NMR that herald a renaissance in which a number of its most important applications reflect the broad problem-solving capability displayed by this method during its classical era during the 1970s and early 1980s.

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Journal ArticleDOI

Nuclear Magnetic Resonance

J. Lee
- 01 May 1968 - 
TL;DR: Emsley and Waugh as mentioned in this paper published the Guide to the NMR Empirical Method A Workbook, which is based on the Bible jun.. Pp. xi + 305.
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Molecular basis of MAP kinase regulation

TL;DR: A review of recent crystal structures of MAPK:KIM‐peptide complexes and how residues outside the canonical KIM motif interact with specific MAPKs and contribute further to MAPK selectivity and signaling pathway fidelity is focused on.
Journal ArticleDOI

Bringing Dynamic Molecular Machines into Focus by Methyl-TROSY NMR

TL;DR: Methyl-TROSY (transverse relaxation optimized spectroscopy) NMR is highlighted, which enables the study of such large systems, and it is shown how this emerging technique contributes to an understanding of cellular function and the role of molecular plasticity in regulating an array of biochemical activities.
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Two-Dimensional NMR Lineshape Analysis

TL;DR: A more accurate and convenient method for the analysis of NMR titration experiments, based on the direct quantum mechanical simulation and fitting of entire two-dimensional experiments, is introduced, which is implemented in a new software tool, TITAN (TITration ANalysis).
References
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Journal ArticleDOI

NMR with Proteins and Nucleic Acids

Kurt Wüthrich
- 01 Jan 1986 - 
Book

NMR of proteins and nucleic acids

TL;DR: The NMR Assignment Problem in Biopolymers, two-Dimensional NMR With Proteins and Nucleic Acids, and Sequence-Specific Resonance Assignments.
Journal ArticleDOI

Intrinsically unstructured proteins and their functions.

TL;DR: Many gene sequences in eukaryotic genomes encode entire proteins or large segments of proteins that lack a well-structured three-dimensional fold, whereas others constitute flexible linkers that have a role in the assembly of macromolecular arrays.
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Relaxation Processes in a System of Two Spins

TL;DR: Abragam and Pound's method for the calculation of the longitudinal relaxation time was extended to the transverse relaxation time in this paper, which gave rise to a steady and transient Overhauser effect.
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