Related ArticlesFTIR and NMR studies on the hydration of a high-M(r) subunit of glutenin.
Int J Biol Macromol. 1995 Apr;17(2):74-80
Authors: Belton PS, Colquhoun IJ, Grant A, Wellner N, Field JM, Shewry PR, Tatham AS
The hydration behaviour of a purified high-M(r) subunit of glutenin has been studied using Fourier transform infra-red (FTIR) and nuclear magnetic resonance (NMR) spectroscopy. The water-insoluble protein was examined in an unalkylated form with intermolecular disulfide bonds, and in a reduced and alkylated (unpolymerized) form. Hydration produced a marked increase in chain mobility, especially above a threshold water content of about 37% w/w. NMR experiments also showed that some parts of the chain were held in a much less mobile state, even at higher water contents. Little difference could be seen between alkylated and unalkylated subunits, implying that NMR is sensitive to localized motions, but not to any restrictions imposed by disulfide bridges close to the chain ends. FTIR spectra of the protein films have shown that increasing hydration enables changes to occur in favour of a more extended and beta-sheet-type structure. The changes in secondary structure are very noticeable at water contents corresponding to the NMR mobility threshold. The behaviour is influenced by intermolecular interactions. beta-sheet formation is enhanced by the presence of disulfide bonds in the unalkylated samples. There is little evidence of beta-structure (sheet or extended chain) either in the dry state, where protein-protein interactions are strongest, or in dilute acetic acid solution, where the interactions are weakest. The balance between protein-protein and protein-water hydrogen-bonding interactions therefore appears to influence the formation of beta-sheet and extended chain structures, and these may in turn affect the elasticity of high M(r) subunits.
[NMR paper] Subunit A of the E. coli ATP synthase: reconstitution and high resolution NMR with pr
Subunit A of the E. coli ATP synthase: reconstitution and high resolution NMR with protein purified in a mixed polarity solvent.
Related Articles Subunit A of the E. coli ATP synthase: reconstitution and high resolution NMR with protein purified in a mixed polarity solvent.
FEBS Lett. 2004 Jan 2;556(1-3):35-8
Authors: Dmitriev OY, Altendorf K, Fillingame RH
Subunit a of the Escherichia coli ATP synthase, a 30 kDa integral membrane protein, was purified to homogeneity by a novel procedure incorporating selective extraction into a monophasic...
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[NMR paper] NMR studies of protein hydration and TEMPOL accessibility.
NMR studies of protein hydration and TEMPOL accessibility.
Related Articles NMR studies of protein hydration and TEMPOL accessibility.
J Mol Biol. 2003 Sep 12;332(2):437-47
Authors: Niccolai N, Spiga O, Bernini A, Scarselli M, Ciutti A, Fiaschi I, Chiellini S, Molinari H, Temussi PA
Understanding the mechanisms of the interaction between a protein surface and its outer molecular environment is of primary relevance for the rational design of new drugs and engineered proteins. Protein surface accessibility is emerging as a new dimension of...
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[NMR paper] Study of wheat high molecular weight 1Dx5 subunit by (13)C and (1)H solid-state NMR.
Study of wheat high molecular weight 1Dx5 subunit by (13)C and (1)H solid-state NMR. II. Roles of nonrepetitive terminal domains and length of repetitive domain.
Related Articles Study of wheat high molecular weight 1Dx5 subunit by (13)C and (1)H solid-state NMR. II. Roles of nonrepetitive terminal domains and length of repetitive domain.
Biopolymers. 2002 Oct 15;65(2):158-68
Authors: Alberti E, Gilbert SM, Tatham AS, Shewry PR, Naito A, Okuda K, Saitô H, Gil AM
This work follows a previous article that addressed the role of disulfide bonds in...
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[NMR paper] Study of high molecular weight wheat glutenin subunit 1Dx5 by 13C and 1H solid-state
Study of high molecular weight wheat glutenin subunit 1Dx5 by 13C and 1H solid-state NMR spectroscopy. I. Role of covalent crosslinking.
Related Articles Study of high molecular weight wheat glutenin subunit 1Dx5 by 13C and 1H solid-state NMR spectroscopy. I. Role of covalent crosslinking.
Biopolymers. 2002;67(6):487-98
Authors: Alberti E, Gilbert SM, Tatham AS, Shewry PR, Gil AM
This work describes a carbon and proton solid-state NMR study of the hydration of a high molecular weight wheat glutenin subunit, 1Dx5. The effect of the presence of...
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[NMR paper] NMR studies of protein hydration.
NMR studies of protein hydration.
Related Articles NMR studies of protein hydration.
Prog Biophys Mol Biol. 1994;61(1):61-79
Authors: Belton PS
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[NMR paper] NMR studies of protein hydration.
NMR studies of protein hydration.
Related Articles NMR studies of protein hydration.
Prog Biophys Mol Biol. 1994;61(1):61-79
Authors: Belton PS
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[NMR paper] 1H NMR studies on the catalytic subunit of aspartate transcarbamoylase.
1H NMR studies on the catalytic subunit of aspartate transcarbamoylase.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles 1H NMR studies on the catalytic subunit of aspartate transcarbamoylase.
Proc Natl Acad Sci U S A. 1992 Dec 15;89(24):11881-5
Authors: Cohen RE, Takama M, Schachman HK
The 1H NMR spectrum of the catalytic subunit of Escherichia coli aspartate transcarbamoylase (EC 2.1.3.2) was simplified by using strains auxotrophic for the aromatic amino...
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[NMR paper] Structural effects of hydration: studies of lysozyme by 13C solids NMR.
Structural effects of hydration: studies of lysozyme by 13C solids NMR.
Related Articles Structural effects of hydration: studies of lysozyme by 13C solids NMR.
Biopolymers. 1990 Dec;29(14):1801-6
Authors: Kennedy SD, Bryant RG
13C-nmr spectra of lysozyme obtained at 50.3 MHz using both static and magic-angle-spinning-cross-polarization methods are reported at several water contents. The line widths and consequent resolution in the hydrated material is substantially improved over that in the lyophilized protein. The line narrowing is not...
FTIR and NMR studies on the hydration of a high-M(r) subunit of glutenin.
Linear Mode
