Related ArticlesComparison of protein structures in solution using local conformations derived from NMR data: application to cytochrome c.
J Biomol Struct Dyn. 1994 Dec;12(3):527-58
Authors: Kar L, Sherman SA, Johnson ME
Structural comparisons of proteins in solution are often required to examine structure-functional relationships, study structural effects of mutations or distinguish between various forms of the same molecule under different conditions. A nuclear magnetic resonance (NMR) based probabilistic strategy is presented and used to study the structural differences between the two redox states of cytochrome c in solution. A probabilistic approach is employed to calculate the main chain conformations of horse ferro- and ferricytochrome c in solution, based on the published sequential d connectivity data. Conformational differences between the two oxidation states of horse cytochrome c in solution are found to be statistically significant. The largest changes in conformation are at residues Lys27, Thr28, Leu32, Gln42, Thr47, Tyr48, Thr49, Glu69, Lys72, Met80, Phe82, Ile85 and Lys86, all of which are close to the heme (within 14 A of the heme iron in the high resolution Xray structure of tuna cytochrome c). We suggest that these conformational changes may modulate local dipole moments and hence influence the interactions of cytochrome c with its physiological redox partners during the electron transfer process. The oxidation state dependent conformational differences are found to be much greater in solution than in the crystalline state, and the solution and crystal structures differ significantly in regions close to the heme. These results suggest that the highly charged nature of cytochrome c makes this protein particularly sensitive to the ionic strength of its environment and leads to differences between crystal and solution structures in the same oxidation state. In such cases, crystal structures must be used with caution for modeling molecular interactions in vivo. More generally, this analysis indicates that the determination of accurate local conformations based on nmr data can provide useful information about structure-functional aspects of proteins in solution.
[NMR paper] Comparison of X-ray and NMR structures: is there a systematic difference in residue contacts between X-ray- and NMR-resolved protein structures?
Comparison of X-ray and NMR structures: is there a systematic difference in residue contacts between X-ray- and NMR-resolved protein structures?
Related Articles Comparison of X-ray and NMR structures: is there a systematic difference in residue contacts between X-ray- and NMR-resolved protein structures?
Proteins. 2005 Jul 1;60(1):139-47
Authors: Garbuzynskiy SO, Melnik BS, Lobanov MY, Finkelstein AV, Galzitskaya OV
We have compared structures of 78 proteins determined by both NMR and X-ray methods. It is shown that X-ray and NMR structures...
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[NMR paper] Comparison of protein backbone entropy and beta-sheet stability: NMR-derived dynamics
Comparison of protein backbone entropy and beta-sheet stability: NMR-derived dynamics of protein G B1 domain mutants.
Related Articles Comparison of protein backbone entropy and beta-sheet stability: NMR-derived dynamics of protein G B1 domain mutants.
J Am Chem Soc. 2001 Jan 10;123(1):185-6
Authors: Stone MJ, Gupta S, Snyder N, Regan L
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[NMR paper] Comparison of the solution conformations of a human immunodeficiency virus peptidomim
Comparison of the solution conformations of a human immunodeficiency virus peptidomimetic and its retro-inverso isomer using 1H NMR spectroscopy.
Related Articles Comparison of the solution conformations of a human immunodeficiency virus peptidomimetic and its retro-inverso isomer using 1H NMR spectroscopy.
J Pept Res. 1997 Dec;50(6):421-35
Authors: Higgins KA, Bicknell W, Keah HH, Hearn MT
The solution conformations of the all L-alpha-peptide 1 and the corresponding retro-all D-alpha-peptide 2, two 20-metric peptides which generate antibodies...
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[NMR paper] Comparison of the NMR and X-ray structures of the HIV-1 matrix protein: evidence for
Comparison of the NMR and X-ray structures of the HIV-1 matrix protein: evidence for conformational changes during viral assembly.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Comparison of the NMR and X-ray structures of the HIV-1 matrix protein: evidence for conformational changes during viral assembly.
Protein Sci. 1996...
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[NMR paper] NMR-derived solution conformations of a hybrid synthetic peptide containing multiple
NMR-derived solution conformations of a hybrid synthetic peptide containing multiple epitopes of envelope protein gp120 from the RF strain of human immunodeficiency virus.
Related Articles NMR-derived solution conformations of a hybrid synthetic peptide containing multiple epitopes of envelope protein gp120 from the RF strain of human immunodeficiency virus.
Biochemistry. 1994 Mar 1;33(8):2055-62
Authors: de Lorimier R, Moody MA, Haynes BF, Spicer LD
Solution conformations of a 40-residue hybrid peptide containing T-helper epitopes and B-cell...
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[NMR paper] NMR-derived solution conformations of a hybrid synthetic peptide containing multiple
NMR-derived solution conformations of a hybrid synthetic peptide containing multiple epitopes of envelope protein gp120 from the RF strain of human immunodeficiency virus.
Related Articles NMR-derived solution conformations of a hybrid synthetic peptide containing multiple epitopes of envelope protein gp120 from the RF strain of human immunodeficiency virus.
Biochemistry. 1994 Mar 1;33(8):2055-62
Authors: de Lorimier R, Moody MA, Haynes BF, Spicer LD
Solution conformations of a 40-residue hybrid peptide containing T-helper epitopes and B-cell...
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[NMR paper] Comparison of protein structures determined by NMR in solution and by X-ray diffracti
Comparison of protein structures determined by NMR in solution and by X-ray diffraction in single crystals.
Related Articles Comparison of protein structures determined by NMR in solution and by X-ray diffraction in single crystals.
Q Rev Biophys. 1992 Aug;25(3):325-77
Authors: Billeter M
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[NMR paper] Solution structures of human transforming growth factor alpha derived from 1H NMR dat
Solution structures of human transforming growth factor alpha derived from 1H NMR data.
Related Articles Solution structures of human transforming growth factor alpha derived from 1H NMR data.
Biochemistry. 1990 Aug 28;29(34):7805-13
Authors: Kline TP, Brown FK, Brown SC, Jeffs PW, Kopple KD, Mueller L
The 600-MHz 1H NMR spectrum of the des-Val-Val mutant of human transforming growth factor alpha (TGF-alpha) was reassigned at pH = 6.3. The conformation space of des-Val-Val TGF-alpha was explored by distance geometry embedding followed by...