Pages: 12. Rene Andrae, Tim Schulze-Hartung, Peter Melchior et al.
Reduced chi-squared is a very popular method for model assessment, model comparison, convergence diagnostic, and error estimation in astronomy. In this manuscript, we discuss the pitfalls involved in using reduced chi-squared. There are two independent problems: (a) The number of degrees of freedom can only be estimated for linear models. Concerning nonlinear models, the number of degrees of freedom is unknown, i.e., it is not possible to compute the value of reduced chi-squared. (b) Due to random noise in the data, also the value of reduced chi-squared itself is subject to noise, i.e., the value is uncertain. This uncertainty impairs the usefulness of reduced chi-squared for differentiating between models or assessing convergence of a minimisation procedure. The impact of noise on the value of reduced chi-squared is surprisingly large, in particular for small data sets, which are very common in astrophysical problems. We conclude that reduced chi-squared can only be used with due caution for linear models, whereas it must not be used for nonlinear models at all. Finally, we recommend more sophisticated and reliable methods, which are also applicable to nonlinear models.
Reduced dimensionality 3D HNCAN for unambiguous HN, CA and N assignment in proteins
Reduced dimensionality 3D HNCAN for unambiguous HN, CA and N assignment in proteins
Publication year: 2012
Source:Journal of Magnetic Resonance</br>
Manoj Kumar Rout, Pushpa Mishra, Hanudatta S. Atreya, Ramakrishna V. Hosur</br>
We present here an improvisation of HNN (Panchal, Bhavesh et al., 2001) called RD 3D HNCAN for backbone (HN, CA and 15N) assignment in both folded and unfolded proteins. This is a reduced dimensionality experiment which employs CA chemical shifts to improve dispersion. Distinct positive and negative peak patterns of various triplet segments...
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03-09-2012 09:16 AM
Reduced dimensionality 3D HNCANfor unambiguous HN, CA and N assignment in proteins
Reduced dimensionality 3D HNCANfor unambiguous HN, CA and N assignment in proteins
Publication year: 2012
Source: Journal of Magnetic Resonance, Available online 8 February 2012</br>
Manoj Kumar*Rout, Pushpa*Mishra, Hanudatta S.*Atreya, Ramakrishna V.*Hosur</br>
We present here an improvisation of HNN (Panchal, Bhavesh et al. 2001)called RD 3D HNCANfor backbone (HN, CA andN) assignment inboth folded and unfolded proteins. This is a reduced dimensionality experiment which employsCAchemical shifts to improve dispersion. Distinct positive and negative peak patternsof various triplet...
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02-10-2012 09:13 AM
Efficient sequential assignments in proteins with reduced dimensionality 3D HN(CA)NH
Efficient sequential assignments in proteins with reduced dimensionality 3D HN(CA)NH
Abstract We present reduced dimensionality (RD) 3D HN(CA)NH for efficient sequential assignment in proteins. The experiment correlates the 15N and 1H chemical shift of a residue (â??iâ??) with those of its immediate N-terminal (i â?? 1) and C-terminal (i + 1) neighbors and provides four-dimensional chemical shift correlations rapidly with high resolution. An assignment strategy is presented which combines the correlations observed in this experiment with amino acid type information obtained from 3D ...
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01-09-2012 08:08 AM
[CNS Yahoo group] Reduced PDBe services between 23 December and 10 January
Reduced PDBe services between 23 December and 10 January
Hi all, This is to inform PDB/EMDB depositors (at PDBe only) and users of PDBe services (http://pdbe.org/) that we will be operating with a reduced level of
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12-23-2010 02:43 AM
[NMR paper] 13C-, 15N- and 31P-NMR studies of oxidized and reduced low molecular mass thioredoxin
13C-, 15N- and 31P-NMR studies of oxidized and reduced low molecular mass thioredoxin reductase and some mutant proteins.
Related Articles 13C-, 15N- and 31P-NMR studies of oxidized and reduced low molecular mass thioredoxin reductase and some mutant proteins.
Eur J Biochem. 2004 Apr;271(8):1437-52
Authors: Eisenreich W, Kemter K, Bacher A, Mulrooney SB, Williams CH, Müller F
Thioredoxin reductase (TrxR) from Escherichia coli, the mutant proteins E159Y and C138S, and the mutant protein C138S treated with phenylmercuric acetate were...
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11-24-2010 09:51 PM
[NMR paper] A proton-NMR investigation of the fully reduced cytochrome c7 from Desulfuromonas ace
A proton-NMR investigation of the fully reduced cytochrome c7 from Desulfuromonas acetoxidans. Comparison between the reduced and the oxidized forms.
Related Articles A proton-NMR investigation of the fully reduced cytochrome c7 from Desulfuromonas acetoxidans. Comparison between the reduced and the oxidized forms.
Eur J Biochem. 1999 Dec;266(2):634-43
Authors: Assfalg M, Banci L, Bertini I, Bruschi M, Giudici-Orticoni MT, Turano P
The solution structure via 1H NMR of the fully reduced form of cytochrome c7 has been obtained. The protein...
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11-18-2010 08:31 PM
[NMR paper] 1H NMR Study of the Reduced Cytochrome c' from Rhodopseudomonas palustris Containing
1H NMR Study of the Reduced Cytochrome c' from Rhodopseudomonas palustris Containing a High-Spin Iron(II) Heme Moiety.
Related Articles 1H NMR Study of the Reduced Cytochrome c' from Rhodopseudomonas palustris Containing a High-Spin Iron(II) Heme Moiety.
Inorg Chem. 1998 Sep 21;37(19):4814-4821
Authors: Bertini I, Dikiy A, Luchinat C, Macinai R, Viezzoli MS
The assignment of the hyperfine shifted signals of the reduced cytochrome c' from Rhodopseudomonas palustris has been obtained through saturation transfer experiments with assigned signals...
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11-17-2010 11:15 PM
[NMR paper] 1H-NMR studies on partially and fully reduced 2(4Fe-4S) ferredoxin from Clostridium p
1H-NMR studies on partially and fully reduced 2(4Fe-4S) ferredoxin from Clostridium pasteurianum.
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 1H-NMR studies on partially and fully reduced 2(4Fe-4S) ferredoxin from Clostridium pasteurianum.
Eur J Biochem. 1992 Mar 1;204(2):831-9
Authors: Bertini I, Briganti F, Luchinat C, Messori L, Monnanni R, Scozzafava A, Vallini G
The ferredoxin from Clostridium pasteurianum, containing two...