Erratic proteins: New insights into a transport mechanism - Phys.Org
Erratic proteins: New insights into a transport mechanism Phys.Org
"Only through employing modern nuclear magnetic resonance spectroscopy, it has become possible to detect this dynamic behavior within Skp." Transporting the membrane protein in such a changing state does not require energy and allows for its rapid ...
Erratic proteins: New insights into a transport mechanism - Phys.Org More...
Did you find this post helpful? |
Similar Threads
Thread
Thread Starter
Forum
Replies
Last Post
New analysis shows how proteins shift into working mode - Phys.Org
<img alt="" height="1" width="1" />
New analysis shows how proteins shift into working mode
Phys.Org
For more than 50 years, scientists around the world have combined experimental techniques such as X-ray crystallography and nuclear magnetic resonance imaging with computer algorithms to determine the three-dimensional structure of proteins.
New analysis shows how proteins shift into working mode - Phys.Org
More...
nmrlearner
Online News
0
08-09-2013 08:00 PM
A trick to fold proteins more quickly - PhysOrg.com - Phys.Org
<img alt="" height="1" width="1" />
A trick to fold proteins more quickly - PhysOrg.com
Phys.Org
"We exploit the experimental data obtained observing the proteins through nuclear magnetic resonance, and use them to create restraints to be applied to the model", explained Laio, who has coordinated the research published in Proceedings of the ...
A trick to fold proteins more quickly - PhysOrg.com - Phys.Org
More...
nmrlearner
Online News
0
05-08-2013 02:49 PM
Intrinsically disordered proteins: A conversation with Rohit Pappu - Phys.Org
Intrinsically disordered proteins: A conversation with Rohit Pappu - Phys.Org
<img alt="" height="1" width="1" />
Intrinsically disordered proteins: A conversation with Rohit Pappu
Phys.Org
The earliest clue was that some protein segments didn't show up in X-ray crystallography or NMR studies, the standard ways of studying protein structure. By the 1990s people who studied how proteins interact with DNA had noticed the proteins often ...
and more »
Read here
nmrlearner
Online News
0
09-20-2012 06:36 PM
Speeding up drug discovery with rapid 3-D mapping of proteins - Phys.Org
<img alt="" height="1" width="1" />
Speeding up drug discovery with rapid 3-D mapping of proteins
Phys.Org
These amino acids gave off telltale structural clues when analyzed with nuclear magnetic resonance spectroscopy, a method for using the magnetic properties of atoms to determine a molecule's physical and chemical properties. "It was very difficult and ...
and more »
Speeding up drug discovery with rapid 3-D mapping of proteins - Phys.Org
More...
nmrlearner
Online News
0
05-30-2012 03:00 PM
[NMR paper] Thermodynamic insights into proteins from NMR spin relaxation studies.
Thermodynamic insights into proteins from NMR spin relaxation studies.
Related Articles Thermodynamic insights into proteins from NMR spin relaxation studies.
Curr Opin Struct Biol. 2001 Oct;11(5):555-9
Authors: Spyracopoulos L, Sykes BD
NMR spin relaxation measurements of picosecond to nanosecond timescale backbone and sidechain fluctuations of protein molecules, and subsequent entropic interpretation yield interesting, but sometimes counterintuitive, insights into proteins. The stabilities of proteins and protein interactions are achieved...
nmrlearner
Journal club
0
11-19-2010 08:44 PM
[NMR paper] Weak substrate binding to transport proteins studied by NMR.
Weak substrate binding to transport proteins studied by NMR.
Related Articles Weak substrate binding to transport proteins studied by NMR.
Biophys J. 1998 Dec;75(6):2794-800
Authors: Spooner PJ, O'Reilly WJ, Homans SW, Rutherford NG, Henderson PJ, Watts A
The weak binding of sugar substrates fails to induce any quantifiable physical changes in the L-fucose-H+ symport protein, FucP, from Escherichia coli, and this protein lacks any strongly binding ligands for competitive binding assays. Access to substrate binding behavior is however possible...
nmrlearner
Journal club
0
11-17-2010 11:15 PM
[NMR paper] Insights into the mechanism of heterodimerization from the 1H-NMR solution structure
Insights into the mechanism of heterodimerization from the 1H-NMR solution structure of the c-Myc-Max heterodimeric leucine zipper.
Related Articles Insights into the mechanism of heterodimerization from the 1H-NMR solution structure of the c-Myc-Max heterodimeric leucine zipper.
J Mol Biol. 1998 Aug 7;281(1):165-81
Authors: Lavigne P, Crump MP, Gagné SM, Hodges RS, Kay CM, Sykes BD
The oncoprotein c-Myc (a member of the helix-loop-helix-leucine zipper (b-HLH-LZ) family of transcription factors) must heterodimerize with the b-HLH-LZ Max...
nmrlearner
Journal club
0
11-17-2010 11:15 PM
Insights into the Mechanism of Ligand Binding to Octopine Dehydrogenase from Pecten m
Insights into the Mechanism of Ligand Binding to Octopine Dehydrogenase from Pecten maximus by NMR and Crystallography.
Related Articles Insights into the Mechanism of Ligand Binding to Octopine Dehydrogenase from Pecten maximus by NMR and Crystallography.
PLoS One. 2010;5(8):
Authors: Smits SH, Meyer T, Mueller A, van Os N, Stoldt M, Willbold D, Schmitt L, Grieshaber MK
Octopine dehydrogenase (OcDH) from the adductor muscle of the great scallop, Pecten maximus, catalyzes the NADH dependent, reductive condensation of L-arginine and pyruvate to...