Related ArticlesEffects of remote mutation on the autolysis of HIV-1 PR: X-ray and NMR investigations.
Biochem Biophys Res Commun. 2002 Jun 7;294(2):395-401
Authors: Kumar M, Kannan KK, Hosur MV, Bhavesh NS, Chatterjee A, Mittal R, Hosur RV
Autolysis rates of the C95M and C95M/C1095A mutants of a HIV-1 protease tethered dimer have been determined by real time NMR and it is observed that the double mutant has approximately two times higher rate. X-ray structure of the C95M/C1095A double mutant has been solved and refined to 2.1 A resolution. Comparison of the double mutant structure with that of C95M single mutant reveals that there is a shift in the position of the catalytic aspartates and the bound catalytic water. The mutation also causes a loss of hydrophobic packing near the dimerization domain of the protein. These observations demonstrate that subtle changes are adequate to cause significant changes in the rate of autolysis of the double mutant. This provides a rationale for the effects of remote mutations on the activity and drug resistance of the enzyme.
[NMR paper] Val(659)-->Glu mutation within the transmembrane domain of ErbB-2: effects measured b
Val(659)-->Glu mutation within the transmembrane domain of ErbB-2: effects measured by (2)H NMR in fluid phospholipid bilayers.
Related Articles Val(659)-->Glu mutation within the transmembrane domain of ErbB-2: effects measured by (2)H NMR in fluid phospholipid bilayers.
Biochemistry. 2000 May 30;39(21):6572-80
Authors: Sharpe S, Barber KR, Grant CW
Certain point mutations within the hydrophobic transmembrane domains of class I receptor tyrosine kinases have been associated with oncogenic transformation in vitro and in vivo . An important...
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11-18-2010 09:15 PM
On the measurement of 15N-{1H} nuclear Overhauser effects. 2. Effects of the saturati
On the measurement of 15N-{1H} nuclear Overhauser effects. 2. Effects of the saturation scheme and water signal suppression
Publication year: 2010
Source: Journal of Magnetic Resonance, In Press, Accepted Manuscript, Available online 24 September 2010</br>
Fabien, Ferrage , Amy, Reichel , Shibani, Battacharya , David, Cowburn , Ranajeet, Ghose</br>
Measurement of steady-state 15N-{1H} nuclear Overhauser effects forms a cornerstone of most methods to determine protein backbone dynamics from spin-relaxation data, since it is the most reliable probe of very fast motions on the ps-ns...
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09-25-2010 07:47 AM
[NMR paper] Trp128Tyr mutation in the N-lobe of recombinant human serum transferrin: 1H- and 15N-
Trp128Tyr mutation in the N-lobe of recombinant human serum transferrin: 1H- and 15N-NMR and metal binding studies.
Related Articles Trp128Tyr mutation in the N-lobe of recombinant human serum transferrin: 1H- and 15N-NMR and metal binding studies.
Protein Eng. 1997 May;10(5):583-91
Authors: Beatty EJ, Cox MC, Frenkiel TA, He QY, Mason AB, Sadler PJ, Tucker A, Woodworth RC
The conserved Trp residue within helix 5 of the N-lobe of human serum transferrin (hTF/2N, 40 kDa) has been mutated to Tyr. NMR and CD spectra and energy calculations show...
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08-22-2010 03:31 PM
[NMR paper] The effects of proteins on [Ca2+] measurement: different effects on fluorescent and N
The effects of proteins on measurement: different effects on fluorescent and NMR methods.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles The effects of proteins on measurement: different effects on fluorescent and NMR methods.
Cell Calcium. 1996 Nov;20(5):425-30
Authors: Matsuda S, Kusuoka H, Hashimoto K, Tsujimura E, Nishimura T
Previous reports showed that the presence of proteins shifts the apparent dissociation constant (Kd) of a fluorescent dye indicator to...
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08-22-2010 02:20 PM
[NMR paper] 13C NMR study of the effects of mutation on the tryptophan dynamics in chymotrypsin i
13C NMR study of the effects of mutation on the tryptophan dynamics in chymotrypsin inhibitor 2: correlations with structure and stability.
Related Articles 13C NMR study of the effects of mutation on the tryptophan dynamics in chymotrypsin inhibitor 2: correlations with structure and stability.
Biochemistry. 1993 Jan 19;32(2):657-62
Authors: Matthews SJ, Jandu SK, Leatherbarrow RJ
Recombinant chymotrypsin inhibitor 2 (CI-2) and the three mutants Ile39-->Val, Ile39-->Leu, and Arg67-->Ala were successfully enriched with tryptophan at position...
Prediction of protein stability after mutation
If you want to make a mutation in your protein to make it behave better in NMR tube, you may consider predicting the change of protein stability and function upon the mutation...it may help to prevent months of wasted time.
Check these web servers: StabilityI-Mutant 2.0
Fold-X
PoPMuSiC
MUpro
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PolyPhen