Characterizing Hydrodynamic Changes during Cation-Binding to Proteins - Azom.com
Characterizing Hydrodynamic Changes during Cation-Binding to Proteins - Azom.com
Azom.com Characterizing Hydrodynamic Changes during Cation-Binding to Proteins Azom.com
The data thus obtained were utilized to produce the distribution of electrophoretic mobility of each state of RCS and RCL. Nuclear Magnetic Resonance Spectroscopy (NMR), Circular Dichroism (CD), and Analytical Ultracentrifugation (AUC) were other ...
[NMR paper] Probing the cation binding modes of macrocyclic HCV protease inhibitor BILN 2061 by multinuclear NMR.
Probing the cation binding modes of macrocyclic HCV protease inhibitor BILN 2061 by multinuclear NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Probing the cation binding modes of macrocyclic HCV protease inhibitor BILN 2061 by multinuclear NMR.
J Pharm Biomed Anal. 2012 Nov;70:609-13
Authors: Busacca CA, Jones PJ, Campbell SJ, Saha AK, Gonnella NC, Senanayake CH
Abstract
The ability of the macrocyclic HCV protease inhibitor BILN 2061 to bind different...
nmrlearner
Journal club
0
02-09-2013 12:18 AM
Superconducting Magnets Used to Observe Proteins, Atom-by-Atom - Azom.com
Superconducting Magnets Used to Observe Proteins, Atom-by-Atom - Azom.com
http://www.bionmr.com//nt3.ggpht.com/news/tbn/t4dz7XpX589ZcM/6.jpg
Azom.com
<img alt="" height="1" width="1" />
Superconducting Magnets Used to Observe Proteins, Atom-by-Atom
Azom.com
â??This is a very specialized facility,â?? says Stanley Opella, professor of chemistry and biochemistry and director of the Center for NMR Spectroscopy and Imaging of Proteins, the organization that operates this building. The purpose of the facility is to ...
nmrlearner
Online News
0
10-27-2012 03:04 AM
[NMR paper] Interpretation of 15N NMR relaxation data of globular proteins using hydrodynamic cal
Interpretation of 15N NMR relaxation data of globular proteins using hydrodynamic calculations with HYDRONMR.
Related Articles Interpretation of 15N NMR relaxation data of globular proteins using hydrodynamic calculations with HYDRONMR.
J Biomol NMR. 2002 Jun;23(2):139-50
Authors: Bernadó P, García de la Torre J, Pons M
HYDRONMR is an implementation of state of the art hydrodynamic modeling to calculate the spectral density functions for NH or C(alpha)-H vectors in a rigid protein structure starting from an atomic level representation. Thus...
nmrlearner
Journal club
0
11-24-2010 08:49 PM
[NMR paper] Hydrodynamic radii of native and denatured proteins measured by pulse field gradient
Hydrodynamic radii of native and denatured proteins measured by pulse field gradient NMR techniques.
Related Articles Hydrodynamic radii of native and denatured proteins measured by pulse field gradient NMR techniques.
Biochemistry. 1999 Dec 14;38(50):16424-31
Authors: Wilkins DK, Grimshaw SB, Receveur V, Dobson CM, Jones JA, Smith LJ
Pulse field gradient NMR methods have been used to determine the effective hydrodynamic radii of a range of native and nonnative protein conformations. From these experimental data, empirical relationships...
nmrlearner
Journal club
0
11-18-2010 08:31 PM
Scientist develops new, innovative methods for characterizing proteins - Eureka! Scie
Scientist develops new, innovative methods for characterizing proteins - Eureka! Science News
http://nt1.ggpht.com/news/tbn/sQ4HHoCA4rXUpM/6.jpg
Eureka! Science News
<img alt="" height="1" width="1" />
Scientist develops new, innovative methods for characterizing proteins
Eureka! Science News
Nuclear magnetic resonance (NMR) data are first collected for a particular protein that is being analyzed. (NMR is a research tool that utilizes high ...
and more »
nmrlearner
NMR research groups
0
10-20-2010 06:50 AM
[NMR paper] Characterizing the use of perdeuteration in NMR studies of large proteins: 13C, 15N a
Characterizing the use of perdeuteration in NMR studies of large proteins: 13C, 15N and 1H assignments of human carbonic anhydrase II.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Characterizing the use of perdeuteration in NMR studies of large proteins: 13C, 15N and 1H assignments of human carbonic anhydrase II.
J Mol Biol. 1996 Dec 20;264(5):1101-16
Authors: Venters RA, Farmer BT, Fierke CA, Spicer LD
Perdeuteration of all non-exchangeable proton sites can...
nmrlearner
Journal club
0
08-22-2010 02:20 PM
[NMR paper] The identification of cation-binding domains on the surface of microsomal cytochrome
The identification of cation-binding domains on the surface of microsomal cytochrome b5 using 1H-NMR paramagnetic difference spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles The identification of cation-binding domains on the surface of microsomal cytochrome b5 using 1H-NMR paramagnetic difference spectroscopy.
Eur J Biochem. 1992 Jan 15;203(1-2):211-23
Authors: Whitford D
One-dimensional and two-dimensional 1H-NMR...
nmrlearner
Journal club
0
08-21-2010 11:41 PM
[NMR paper] Location of a cation-binding site in the loop between helices F and G of bacteriorhod
Location of a cation-binding site in the loop between helices F and G of bacteriorhodopsin as studied by 13C NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-cellhub.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Location of a cation-binding site in the loop between helices F and G of bacteriorhodopsin as studied by 13C NMR.
Biophys J. 1999 Mar;76(3):1523-31
Authors: Tuzi S, Yamaguchi S, Tanio M, Konishi H, Inoue S, Naito A,...
Characterizing Hydrodynamic Changes during Cation-Binding to Proteins - Azom.com
Linear Mode
