Related ArticlesHuman ?B2-Crystallin Forms a Face-en-Face Dimer in Solution: An Integrated NMR and SAXS Study.
Structure. 2017 Feb 16;:
Authors: Xi Z, Whitley MJ, Gronenborn AM
Abstract
??-Crystallins are long-lived eye lens proteins that are crucial for lens transparency and refractive power. Each ??-crystallin comprises two homologous domains, which are connected by a short linker. ?-Crystallins are monomeric, while ?-crystallins crystallize as dimers and multimers. In the crystal, human ?B2-crystallin is a domain-swapped dimer while the N-terminally truncated ?B1-crystallin forms a face-en-face dimer. Combining and integrating data from multi-angle light scattering, nuclear magnetic resonance, and small-angle X-ray scattering of full-length and terminally truncated human ?B2-crystallin in solution, we show that both these ?B2-crystallin proteins are dimeric, possess C2 symmetry, and are more compact than domain-swapped dimers. Importantly, no inter-molecular paramagnetic relaxation enhancement effects compatible with domain swapping were detected. Our collective experimental results unambiguously demonstrate that, in solution, human ?B2-crystallin is not domain swapped and exhibits a face-en-face dimer structure similar to the crystal structure of truncated ?B1-crystallin.
PMID: 28238532 [PubMed - as supplied by publisher]
Nuclear Magnetic Resonance Structure of a Major Lens Protein, Human ?C-Crystallin: Role of the Dipole Moment in Protein Solubility
Nuclear Magnetic Resonance Structure of a Major Lens Protein, Human ?C-Crystallin: Role of the Dipole Moment in Protein Solubility
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.6b00359/20160521/images/medium/bi-2016-00359c_0010.gif
Biochemistry
DOI: 10.1021/acs.biochem.6b00359
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05-23-2016 10:51 PM
[NMR paper] NMR structure of a major lens protein, Human ?C-Crystallin: Role of dipole moment in protein solubility.
NMR structure of a major lens protein, Human ?C-Crystallin: Role of dipole moment in protein solubility.
Related Articles NMR structure of a major lens protein, Human ?C-Crystallin: Role of dipole moment in protein solubility.
Biochemistry. 2016 May 17;
Authors: Dixit K, Pande A, Pande J, Sarma SP
Abstract
A hallmark of the crystallin proteins is their exceptionally high solubility, which is vital for maintaining the high refractive index of the eye lens. Human ?C-crystallin is a major ?-crystallin whose mutant forms are...
TransientElectrostatic Interactions Dominate theConformational Equilibrium Sampled by Multidomain Splicing FactorU2AF65: A Combined NMR and SAXS Study
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Jie-rong Huang, Lisa R. Warner, Carolina Sanchez, Frank Gabel, Tobias Madl, Cameron D. Mackereth, Michael Sattler and Martin Blackledge
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja502030n/aop/images/medium/ja-2014-02030n_0009.gif
Journal of the American Chemical Society
DOI: 10.1021/ja502030n
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[NMR paper] Monitoring the interaction between ?2-microglobulin and the molecular chaperone ?B-crystallin by NMR and mass spectrometry. ?B-Crystallin dissociates ?2-microglobulin oligomers.
Monitoring the interaction between ?2-microglobulin and the molecular chaperone ?B-crystallin by NMR and mass spectrometry. ?B-Crystallin dissociates ?2-microglobulin oligomers.
Related Articles Monitoring the interaction between ?2-microglobulin and the molecular chaperone ?B-crystallin by NMR and mass spectrometry. ?B-Crystallin dissociates ?2-microglobulin oligomers.
J Biol Chem. 2013 May 3;
Authors: Esposito G, Garvey M, Alverdi V, Pettirossi F, Corazza A, Fogolari F, Polano M, Mangione PP, Giorgetti S, Stoppini M, Rekas A, Bellotti V, Heck AJ, Carver JA...
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[NMR paper] Hydrogen bonding on the ice-binding face of a beta-helical antifreeze protein indicat
Hydrogen bonding on the ice-binding face of a beta-helical antifreeze protein indicated by amide proton NMR chemical shifts.
Related Articles Hydrogen bonding on the ice-binding face of a beta-helical antifreeze protein indicated by amide proton NMR chemical shifts.
Biochemistry. 2004 Oct 19;43(41):13012-7
Authors: Daley ME, Graether SP, Sykes BD
The dependence of amide proton chemical shifts on temperature is used as an indication of the hydrogen bonding properties in a protein. The amide proton temperature coefficients of the beta-helical...
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[NMR paper] NMR solution structure of the C-terminal fragment 255-316 of thermolysin: a dimer for
NMR solution structure of the C-terminal fragment 255-316 of thermolysin: a dimer formed by subunits having the native structure.
Related Articles NMR solution structure of the C-terminal fragment 255-316 of thermolysin: a dimer formed by subunits having the native structure.
Biochemistry. 1994 Dec 13;33(49):14834-47
Authors: Rico M, Jiménez MA, González C, De Filippis V, Fontana A
The solution structure of the C-terminal fragment 255-316 of thermolysin has been determined by two-dimensional proton NMR methods. For this disulfide-free...
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[NMR paper] Solid-state 13C and 15N NMR study of the low pH forms of bacteriorhodopsin.
Solid-state 13C and 15N NMR study of the low pH forms of bacteriorhodopsin.
Related Articles Solid-state 13C and 15N NMR study of the low pH forms of bacteriorhodopsin.
Biochemistry. 1990 Jul 24;29(29):6873-83
Authors: de Groot HJ, Smith SO, Courtin J, van den Berg E, Winkel C, Lugtenburg J, Griffin RG, Herzfeld J
The visible absorption of bacteriorhodopsin (bR) is highly sensitive to pH, the maximum shifting from 568 nm (pH 7) to approximately 600 nm (pH 2) and back to 565 nm (pH 0) as the pH is decreased further with HCl. Blue membrane...
Human ?B2-Crystallin Forms a Face-en-Face Dimer in Solution: An Integrated NMR and SAXS Study.
Linear Mode
