NMR-based structural biology of proteins in supercooled water.
J Struct Funct Genomics. 2011 May 1;
Authors: Szyperski T, Mills JL
NMR-based structural biology of proteins can be pursued efficiently in supercooled water at temperatures well below the freezing point of water. This enables one to study protein structure, dynamics, hydration and cold denaturation in an unperturbed aqueous solution at very low temperatures. Furthermore, such studies enable one to accurately measure thermodynamic parameters associated with protein cold denaturation. Presently available approaches to acquire NMR data for supercooled aqueous protein solutions are surveyed, new insights obtained from such studies are summarized, and future perspectives are discussed.
PMID: 21533787 [PubMed - as supplied by publisher]
Research Scientist Position in the Cryo-Electron Microscopy Facility at the New York Structural Biol - New York Structural Biology Center - New York, NY, United States
Research Scientist Position in the Cryo-Electron Microscopy Facility at the New York Structural Biol - New York Structural Biology Center - New York, NY, United States
The New York Structural Biology Center (NYSBC) seeks an experienced electron microscopist to join the staff of its Cryo-Electron Microscope Facility (http://cryoem.nysbc.org). The NYSBC is shared center that supports state-of-the-art research in cryo-EM, NMR, and X-ray. Cryo-EM facilities include four transmission electron microscopes and a new d...
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01-26-2011 04:21 AM
An NMR-Based Structural Rationale for Contrasting Stoichiometry and Ligand Binding Site(s) in Fatty Acid-binding Proteins.
An NMR-Based Structural Rationale for Contrasting Stoichiometry and Ligand Binding Site(s) in Fatty Acid-binding Proteins.
An NMR-Based Structural Rationale for Contrasting Stoichiometry and Ligand Binding Site(s) in Fatty Acid-binding Proteins.
Biochemistry. 2011 Jan 12;
Authors: He Y, Estephan R, Yang X, Vela A, Wang H, Bernard C, Stark RE
Liver fatty acid-binding protein (LFABP) is a 14-kDa cytosolic polypeptide, differing from other family members in number of ligand binding sites, diversity of bound ligands, and transfer of fatty acid(s) to...
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01-14-2011 12:05 PM
Structural biology: Proteins in dynamic equilibrium - Nature.com
Structural biology: Proteins in dynamic equilibrium - Nature.com
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Structural biology: Proteins in dynamic equilibrium
Nature.com
Changes in global orientations of protein domains, or in the shape and size of molecular assemblies, are more difficult to characterize using NMR alone, ...
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12-23-2010 02:43 AM
[NMR paper] Aromatic ring-flipping in supercooled water: implications for NMR-based structural bi
Aromatic ring-flipping in supercooled water: implications for NMR-based structural biology of proteins.
Related Articles Aromatic ring-flipping in supercooled water: implications for NMR-based structural biology of proteins.
J Am Chem Soc. 2001 Jan 24;123(3):388-97
Authors: Skalicky JJ, Mills JL, Sharma S, Szyperski T
We have characterized, for the first time, motional modes of a protein dissolved in supercooled water: the flipping kinetics of phenylalanyl and tyrosinyl rings of the 6 kDa protein BPTI have been investigated by NMR at...
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11-19-2010 08:32 PM
[NMR paper] An account of NMR in structural biology.
An account of NMR in structural biology.
Related Articles An account of NMR in structural biology.
Nat Struct Biol. 1997 Oct;4 Suppl:841-4
Authors: Wagner G
With the ability to determine atomic resolution structures of biological macromolecules in semi-physiological conditions, nuclear magnetic resonance spectroscopy (NMR) has become an eminent tool in structural biology. NMR provides a means for studying critical biological phenomena including protein structure, dynamics and folding as well as a practical approach to drug design.
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08-22-2010 05:08 PM
Prospects for lanthanides in structural biology by NMR
Prospects for lanthanides in structural biology by NMR
Gottfried Otting
Journal of Biomolecular NMR; 2008; 42(1); pp 1-9
Abstract:
The advent of different lanthanide-binding reagents has made site-specific labelling of proteins with paramagnetic lanthanides a viable proposition. This brings many powerful techniques originally established and demonstrated for paramagnetic metalloproteins into the mainstream of structural biology. The promise is that, by exploiting the long-range effects of paramagnetism, lanthanide labelling will allow the study of larger proteins and protein–ligand...
NMR-based structural biology of proteins in supercooled water.
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