✦ LIBER ✦

Dynamic properties of proteins from NMR spectroscopy

✍ Scribed by Arthur G. Palmer III

Publisher: Elsevier Science
Year: 1993
Tongue: English
Weight: 803 KB
Volume: 4
Category: Article
ISSN: 0958-1669
DOI: 10.1016/0958-1669(93)90002-e

No coin nor oath required. For personal study only.

✦ Synopsis

Two-dimensional proton-detected heteronuclear nuclear magnetic resonance spectroscopy has been used to measure 13C and 15N spin-relaxation rate constants for several proteins. Generalized order parameters and effective internal correlation times have been calculated from the relaxation data to characterize intramolecular motions that are more rapid than overall rotational diffusion. These studies provide detailed descriptions of the magnitudes and timescales of fluctuations in protein molecules.

📜 SIMILAR VOLUMES

NMR and dielectric spectroscopy investig

NMR and dielectric spectroscopy investigation of protein dynamical structure.

✍ V.D. Fedotov; Yu.D. Feldman; A.G. Krushelnitsky; I.V. Ermolina 📂 Article 📅 1990 🏛 Elsevier Science 🌐 English ⚖ 317 KB

Structure and dynamics of the DNA bindin

Structure and dynamics of the DNA binding protein HU from Bacillus stearothermophilus by NMR spectroscopy

✍ Rolf Boelens; Hans Vis; Constantin E. Vorgias; Keith S. Wilson; Robert Kaptein 📂 Article 📅 1996 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 570 KB

The DNA-binding protein HU from Bacillus stearothermophilus (HUBst) is a dimer with a molecular weight of 195 kDa that is capable of bending DNA. An x-ray structure has been determined previously [Tanaka et al. 1984) Nature, vol. 310, pp. 376-381], but no structure could be established for a large p

NMR spectroscopy: From quantum mechanics

NMR spectroscopy: From quantum mechanics to protein spectra

✍ Cerf, Corinne 📂 Article 📅 1997 🏛 John Wiley and Sons 🌐 English ⚖ 440 KB

The NMR method is presented, starting from its fundamental physical principles. First, the quantum mechanics formalism is explained, and the concept of the density operator is highlighted. Then, using this formalism, NMR spectra of increasing complexity are considered, from the simple one-dimensiona

Solid-State NMR Spectroscopy of Amyloid

Solid-State NMR Spectroscopy of Amyloid Proteins

✍ Henrike Heise 📂 Article 📅 2008 🏛 John Wiley and Sons 🌐 English ⚖ 631 KB

Backbone dynamics of proteins studied by

Backbone dynamics of proteins studied by two-dimensional heteronuclear NMR spectroscopy and molecular dynamics simulations

✍ David Fushman; Rüdiger Weisemann; Harald Thüring; Oliver Ohlenschläger; Heinz Rü 📂 Article 📅 1996 🏛 John Wiley and Sons 🌐 English ⚖ 883 KB

To investigate the backbone dynamics of roteins I5N longitudinal and transverse relaxation experiments combined with (lH, r5N] NOE measurements together with molecular dynamics simulations were carried out using ribonuclease TI and the complex of ribonuclease TI with 2'GMP as a model protein. The in

Transient complexes of redox proteins: s

Transient complexes of redox proteins: structural and dynamic details from NMR studies

✍ Miguel Prudêncio; Marcellus Ubbink 📂 Article 📅 2004 🏛 John Wiley and Sons 🌐 English ⚖ 447 KB

## Abstract Redox proteins participate in many metabolic routes, in particular those related to energy conversion. Protein–protein complexes of redox proteins are characterized by a weak affinity and a short lifetime. Two‐dimensional NMR spectroscopy has been applied to many redox protein complexes