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Methodological advances in protein NMR
Ad Bax,Stephan Grzesiek +1 more
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TLDR
The present chapter focuses primarily on the methodological advances in this latter application, particularly as they relate to the study of proteins in solution.Abstract:
Since the first experimental observation of nuclear magnetic resonance (NMR) in bulk matter more than 45 years ago (Bloch et al., 1946; Purcell et al., 1946), its history has been punctuated by a series of revolutionary advances that have greatly expanded its horizons. Indeed, methodological and instrumental developments witnessed over the past two decades have turned NMR into the most diverse spectroscopic tool currently available. Applications vary from exploration of natural resources and medical imaging to determination of the three-dimensional structure of biologically important macromolecules (Wuthrich, 1986; Kaptein et al., 1988; Bax, 1989; Clore and Gronenborn, 1989; Markley, 1989; Wuthrich, 1989; Wagner et al., 1992). The present chapter focuses primarily on the methodological advances in this latter application, particularly as they relate to the study of proteins in solution.read more
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Journal ArticleDOI
NMRPipe: a multidimensional spectral processing system based on UNIX pipes
TL;DR: The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks.
Journal ArticleDOI
The program XEASY for computer-supported NMR spectral analysis of biological macromolecules.
TL;DR: XEASY was developed for work with 2D, 3D and 4D NMR data sets to provide maximal computer support for the analysis of spectra, while providing the user with complete control over the final resonance assignments.
Journal ArticleDOI
NMR Solution Structure of the Human Prion Protein
Ralph Zahn,Aizhuo Liu,Thorsten Lührs,Roland Riek,Christine von Schroetter,Francisco López García,Martin Billeter,Luigi Calzolai,Gerhard Wider,Kurt Wüthrich +9 more
TL;DR: The NMR structures of the recombinant human prion protein hPrP(23-230) include a globular domain extending from residues 125-228, for which a detailed structure was obtained, and an N-terminal flexibly disordered "tail," which influences the local conformational state of the polypeptide segments.
Journal ArticleDOI
Solution structure of the KIX domain of CBP bound to the transactivation domain of CREB: a model for activator:coactivator interactions.
Ishwar Radhakrishnan,Gabriela C. Pérez-Alvarado,David Parker,H. Jane Dyson,Marc Montminy,Peter E. Wright +5 more
TL;DR: The solution structure of the complex formed by the phosphorylated kinase-inducible domain (pKID) of CREB with KIX reveals that pKID undergoes a coil-->helix folding transition upon binding to KIX, forming two alpha helices.
Journal ArticleDOI
Release of long-range tertiary interactions potentiates aggregation of natively unstructured α-synuclein
Carlos W. Bertoncini,Young-Sang Jung,Claudio O. Fernández,Wolfgang Hoyer,Christian Griesinger,Thomas M. Jovin,Markus Zweckstetter +6 more
TL;DR: Stabilization of the native, autoinhibitory structure of alphaS constitutes a potential strategy for reducing or inhibiting oligomerization and aggregation in Parkinson's disease.
References
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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
Resonance Absorption by Nuclear Magnetic Moments in a Solid
Book
Principles of nuclear magnetic resonance in one and two dimensions
TL;DR: In this paper, the dynamics of nuclear spin systems were studied by two-dimensional exchange spectroscopy and nuclear magnetic resonance imaging (NEMI) imaging, and two different correlation methods based on coherence transfer were proposed.
Journal ArticleDOI
Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 1. Theory and range of validity
Giovanni Lipari,Attila Szabo +1 more
TL;DR: In this article, a model-free approach to the interpretation of nuclear magnetic resonance relaxation experiments on macromolecules in solution is presented, which uses the above spectral density to least-squares fit relaxation data by treating S/sup 2 and T/sub e/ as adjustable parameters.