[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...
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Scientists Observe Structure of Protein That Plays Major Role in Huntington's Disease, Opening Door to Finding Cause ... - Huntington's Disease News
Scientists Observe Structure of Protein That Plays Major Role in Huntington's Disease, Opening Door to Finding Cause ... - Huntington's Disease News
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Scientists Observe Structure of Protein That Plays Major Role in Huntington's Disease, Opening Door to Finding Cause ...
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Leibniz-Institut für Molekulare Pharmakologie (FMP) researchers used a combination of nuclear magnetic...
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02-10-2016 09:28 PM
[NMR images] ... PROTEIN solubility determined with the OptiSol protein solubility
http://1.bp.blogspot.com/-7csMp0V8hEo/UXsrKtXoTPI/AAAAAAAAAGU/RIaxBdCKiTA/s640/increasing_solubility_fiv_matrix_protein_NMR_optisol.JPG
31/05/2014 1:57:49 PM GMT
... PROTEIN solubility determined with the OptiSol protein solubility
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[NMR paper] The structure and dipole moment of globular proteins in solution and crystalline stat
The structure and dipole moment of globular proteins in solution and crystalline states: use of NMR and X-ray databases for the numerical calculation of dipole moment.
Related Articles The structure and dipole moment of globular proteins in solution and crystalline states: use of NMR and X-ray databases for the numerical calculation of dipole moment.
Biopolymers. 2001 Apr 5;58(4):398-409
Authors: Takashima S
The large dipole moment of globular proteins has been well known because of the detailed studies using dielectric relaxation and...
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11-19-2010 08:32 PM
[NMR paper] The electric dipole moment of DNA-binding HU protein calculated by the use of an NMR
The electric dipole moment of DNA-binding HU protein calculated by the use of an NMR database.
Related Articles The electric dipole moment of DNA-binding HU protein calculated by the use of an NMR database.
Biophys Chem. 1999 Aug 30;80(3):153-63
Authors: Takashima S, Yamaoka K
Electric birefringence measurements indicated the presence of a large permanent dipole moment in HU protein-DNA complex. In order to substantiate this observation, numerical computation of the dipole moment of HU protein homodimer was carried out by using NMR protein...
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[NMR paper] NMR study suggests a major role for Arg111 in maintaining the structure and dynamical
NMR study suggests a major role for Arg111 in maintaining the structure and dynamical properties of type II human cellular retinoic acid binding protein.
Related Articles NMR study suggests a major role for Arg111 in maintaining the structure and dynamical properties of type II human cellular retinoic acid binding protein.
Biochemistry. 1998 Sep 15;37(37):13021-32
Authors: Wang L, Yan H
The solution structure of a site-directed mutant of type-II human cellular retinoic acid binding protein (CRABPII) with Arg111 replaced by methionine (R111M)...
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[NMR paper] 1H-NMR spectroscopy of beta B2-crystallin from bovine eye lens. Conformation of the N
1H-NMR spectroscopy of beta B2-crystallin from bovine eye lens. Conformation of the N- and C-terminal extensions.
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 spectroscopy of beta B2-crystallin from bovine eye lens. Conformation of the N- and C-terminal extensions.
Eur J Biochem. 1993 Apr 1;213(1):313-20
Authors: Carver JA, Cooper PG, Truscott RJ
1H-NMR spectroscopic studies of a 46-kDa homodimer, beta B2-crystallin,...
Nuclear Magnetic Resonance Structure of a Major Lens Protein, Human ?C-Crystallin: Role of the Dipole Moment in Protein Solubility
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