Related ArticlesDefining the statistical distribution of vesicle diameters facilitates quantitative assessment of spectral narrowing from small vesicles in protein/lipid interaction studies by 2H-NMR.
Biochem Biophys Res Commun. 1993 May 14;192(3):1042-8
Authors: Gale P
The diameters of vesicles comprising complexes of an integral membrane protein and 1,2-dimyristoyl-sn-glycero-3-phosphocholine, deuterated in the choline gamma-methyl groups, exhibited a lognormal distribution defined by the geometric mean (GM) and the logarithmic standard deviation (LSD). The range of vesicle sizes within each complex was very large (e.g., 99% of vesicles measured between 60 nm and 4,000 nm in one complex). This complicated assessment of spectral narrowing artefacts from small vesicles in broad line 2H-NMR results. Artefacts (e.g., decreases in quadrupole splitting and generation of two component spectra) resembled results attributed to membrane proteins in other 2H-NMR studies for which spectral narrowing was dismissed by demonstration of some vesicles > 400 nm in diameter. This was inadequate since 2H-NMR spectra from complexes with GM < 350 nm exhibited spectral narrowing artefacts despite the presence of some vesicles 1,200 nm in diameter. The nature and degree of artefact were determined by both GM and LSD. Quantifying vesicle sizes by GM and LSD accommodated the large size variation within a complex and facilitated quantitative assessment of artefacts through comparison of different complexes.
DARS-RNP and QUASI-RNP: New statistical potentials for protein-RNA docking - 7thSpace Interactive (press release)
DARS-RNP and QUASI-RNP: New statistical potentials for protein-RNA docking - 7thSpace Interactive (press release)
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DARS-RNP and QUASI-RNP: New statistical potentials for protein-RNA docking
7thSpace Interactive (press release)
Unfortunately, the experimental determination of protein-RNA complexes is tedious and difficult, both by X-ray crystallography and NMR. For many interacting proteins and RNAs the individual structures are available, enabling computational prediction of ...
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08-19-2011 04:02 AM
[NMR paper] An increase in side chain entropy facilitates effector binding: NMR characterization
An increase in side chain entropy facilitates effector binding: NMR characterization of the side chain methyl group dynamics in Cdc42Hs.
Related Articles An increase in side chain entropy facilitates effector binding: NMR characterization of the side chain methyl group dynamics in Cdc42Hs.
Biochemistry. 2001 Apr 17;40(15):4590-600
Authors: Loh AP, Pawley N, Nicholson LK, Oswald RE
Cdc42Hs is a signal transduction protein that is involved in cytoskeletal growth and organization. We describe here the methyl side chain dynamics of three forms of...
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11-19-2010 08:32 PM
Solid-state NMR characterization of gas vesicle structure.
Solid-state NMR characterization of gas vesicle structure.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-cellhub.gif Related Articles Solid-state NMR characterization of gas vesicle structure.
Biophys J. 2010 Sep 22;99(6):1932-9
Authors: Sivertsen AC, Bayro MJ, Belenky M, Griffin RG, Herzfeld J
Gas vesicles are gas-filled buoyancy organelles with walls that consist almost exclusively of gas vesicle protein A (GvpA). Intact, collapsed gas vesicles from the cyanobacterium Anabaena flos-aquae were studied...
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09-24-2010 03:50 AM
[NMR paper] Defining long range order in NMR structure determination from the dependence of heter
Defining long range order in NMR structure determination from the dependence of heteronuclear relaxation times on rotational diffusion anisotropy.
Related Articles Defining long range order in NMR structure determination from the dependence of heteronuclear relaxation times on rotational diffusion anisotropy.
Nat Struct Biol. 1997 Jun;4(6):443-9
Authors: Tjandra N, Garrett DS, Gronenborn AM, Bax A, Clore GM
Structure determination by NMR presently relies on short range restraints between atoms in close spatial proximity, principally in the...
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08-22-2010 03:31 PM
[NMR paper] Defining long range order in NMR structure determination from the dependence of heter
Defining long range order in NMR structure determination from the dependence of heteronuclear relaxation times on rotational diffusion anisotropy.
Related Articles Defining long range order in NMR structure determination from the dependence of heteronuclear relaxation times on rotational diffusion anisotropy.
Nat Struct Biol. 1997 Jun;4(6):443-9
Authors: Tjandra N, Garrett DS, Gronenborn AM, Bax A, Clore GM
Structure determination by NMR presently relies on short range restraints between atoms in close spatial proximity, principally in the...
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08-22-2010 03:03 PM
[NMR paper] Defining the precision with which a protein structure is determined by NMR. Applicati
Defining the precision with which a protein structure is determined by NMR. Application to motilin.
Related Articles Defining the precision with which a protein structure is determined by NMR. Application to motilin.
Biochemistry. 1993 Feb 16;32(6):1610-7
Authors: Shriver J, Edmondson S
A simple procedure is introduced for accurately defining the precision with which the Cartesian coordinates of any macromolecular structure are determined by nuclear Overhauser data. The method utilizes an ensemble of structures obtained from an array of...
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08-21-2010 11:53 PM
[NMR paper] Completeness of NOEs in protein structure: a statistical analysis of NMR.
Completeness of NOEs in protein structure: a statistical analysis of NMR.
Related Articles Completeness of NOEs in protein structure: a statistical analysis of NMR.
J Biomol NMR. 1999 Jun;14(2):123-32
Authors: Doreleijers JF, Raves ML, Rullmann T, Kaptein R
The completeness of experimentally observed NOE restraints of a set of 97 NMR protein structures deposited in the PDB has been assessed. Completeness is defined as the ratio of the number of experimentally observed NOEs and the number of 'expected NOEs'. A practical definition of 'expected...