[NMR paper] Unveiling the "Three Finger Pharmacophore" required for p53-MDM2 Inhibition by Saturation Transfer Difference NMR Initial Growth Rates Approach.
Unveiling the "Three Finger Pharmacophore" required for p53-MDM2 Inhibition by Saturation Transfer Difference NMR Initial Growth Rates Approach.
Related Articles Unveiling the "Three Finger Pharmacophore" required for p53-MDM2 Inhibition by Saturation Transfer Difference NMR Initial Growth Rates Approach.
Chemistry. 2016 Feb 11;
Authors: Angulo J, Goffin SA, Gandhi D, Searcey M, Howell LA
Abstract
Inhibitors of the p53-MDM2 protein-protein interaction are emerging as a novel and validated approach to treating cancer. In this work...
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02-13-2016 02:40 PM
[NMRpipe Yahoo group] Re: Convering Varian's "S3" spectra
Re: Convering Varian's "S3" spectra
Have a look in the NMRPipe script library graciously maintained by Dr. Ryan McKay and the staff of NANUC ... www.nanuc.ca ... while you're at the web site, you
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03-09-2011 04:19 AM
[NMRpipe Yahoo group] Convering Varian's "S3" spectra
Convering Varian's "S3" spectra
Hello all. I wondering if anyone has conversion scripts for the "spin-state-selective" pulse sequences in Varian's Biopack. These pulse sequences are named
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[NMR paper] Reconstructing NMR spectra of "invisible" excited protein states using HSQC and HMQC
Reconstructing NMR spectra of "invisible" excited protein states using HSQC and HMQC experiments.
Related Articles Reconstructing NMR spectra of "invisible" excited protein states using HSQC and HMQC experiments.
J Am Chem Soc. 2002 Oct 16;124(41):12352-60
Authors: Skrynnikov NR, Dahlquist FW, Kay LE
Carr-Purcell-Meiboom-Gill (CPMG) relaxation measurements employing trains of 180 degrees pulses with variable pulse spacing provide valuable information about systems undergoing millisecond-time-scale chemical exchange. Fits of the CPMG relaxation...
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11-24-2010 08:58 PM
Mechanically, Magnetically, and "Rotationally Aligned" Membrane Proteins in Phospholi
Mechanically, Magnetically, and "Rotationally Aligned" Membrane Proteins in Phospholipid Bilayers Give Equivalent Angular Constraints for NMR Structure Determination.
Related Articles Mechanically, Magnetically, and "Rotationally Aligned" Membrane Proteins in Phospholipid Bilayers Give Equivalent Angular Constraints for NMR Structure Determination.
J Phys Chem B. 2010 Oct 20;
Authors: Park SH, Das BB, De Angelis AA, Scrima M, Opella SJ
The native environment for membrane proteins is the highly asymmetric phospholipid bilayer, and this has a large...
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10-22-2010 04:33 PM
[NMR paper] "Ensemble" iterative relaxation matrix approach: a new NMR refinement protocol applie
"Ensemble" iterative relaxation matrix approach: a new NMR refinement protocol applied to the solution structure of crambin.
Related Articles "Ensemble" iterative relaxation matrix approach: a new NMR refinement protocol applied to the solution structure of crambin.
Proteins. 1993 Apr;15(4):385-400
Authors: Bonvin AM, Rullmann JA, Lamerichs RM, Boelens R, Kaptein R
The structure in solution of crambin, a small protein of 46 residues, has been determined from 2D NMR data using an iterative relaxation matrix approach (IRMA) together with...