The monoclonal antibody (mAb) protein class has become a primary therapeutic platform for the production of new life saving drug products. MAbs are comprised of two domains: the antigen-binding fragment (Fab) and crystallizable fragment (Fc). Despite the success in the clinic, NMR assignments of the complete Fab domain have been elusive, in part due to problems in production of properly folded, triply-labeled ²H,^(13)C,^(15)N Fab domain. Here, we report the successful recombinant expression of a...
[NMR paper] NMR assignment and solution structure of the external DII domain of the yeast Rvb2 protein.
NMR assignment and solution structure of the external DII domain of the yeast Rvb2 protein.
NMR assignment and solution structure of the external DII domain of the yeast Rvb2 protein.
Biomol NMR Assign. 2018 Mar 22;:
Authors: Bragantini B, Rouillon C, Charpentier B, Manival X, Quinternet M
Abstract
We report the nearly complete 1H, 15N and 13C resonance assignment and the solution structure of the external DII domain of the yeast Rvb2 protein, a member of the AAA+ATPase superfamily.
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[NMR paper] Backbone (1)H, (15)N, (13)C NMR assignment of the 518-627 fragment of the androgen receptor encompassing N-terminal and DNA binding domains.
Backbone (1)H, (15)N, (13)C NMR assignment of the 518-627 fragment of the androgen receptor encompassing N-terminal and DNA binding domains.
Related Articles Backbone (1)H, (15)N, (13)C NMR assignment of the 518-627 fragment of the androgen receptor encompassing N-terminal and DNA binding domains.
Biomol NMR Assign. 2016 Jan 5;
Authors: Meyer S, Wang YH, Pérez-Escrivà P, Kieffer B
Abstract
Androgen receptor (AR) belongs to the nuclear receptor superfamily that are ligand dependent transcription factors. This protein binds to...
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01-07-2016 11:10 PM
[NMR paper] Backbone ¹H, ¹³C, ¹?N NMR assignments of yeast OMP synthase in unliganded form and in complex with orotidine 5'-monophosphate.
Backbone ¹H, ¹³C, ¹?N NMR assignments of yeast OMP synthase in unliganded form and in complex with orotidine 5'-monophosphate.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles Backbone ¹H, ¹³C, ¹?N NMR assignments of yeast OMP synthase in unliganded form and in complex with orotidine 5'-monophosphate.
Biomol NMR Assign. 2014 Apr;8(1):103-8
Authors: Hansen MR, Harris R, Barr EW, Cheng H, Girvin ME, Grubmeyer C
Abstract
The...
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11-14-2014 08:33 AM
[NMR paper] Yeast-expressed human membrane protein aquaporin-1 yields excellent resolution of solid-state MAS NMR spectra.
Yeast-expressed human membrane protein aquaporin-1 yields excellent resolution of solid-state MAS NMR spectra.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles Yeast-expressed human membrane protein aquaporin-1 yields excellent resolution of solid-state MAS NMR spectra.
J Biomol NMR. 2013 Jan 24;
Authors: Emami S, Fan Y, Munro R, Ladizhansky V, Brown LS
Abstract
One of the biggest challenges in solid-state NMR studies of membrane proteins is to obtain a...
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02-03-2013 10:19 AM
RDC derived protein backbone resonance assignment using fragment assembly
RDC derived protein backbone resonance assignment using fragment assembly
Abstract Experimental residual dipolar couplings (RDCs) in combination with structural models have the potential for accelerating the protein backbone resonance assignment process because RDCs can be measured accurately and interpreted quantitatively. However, this application has been limited due to the need for very high-resolution structural templates. Here, we introduce a new approach to resonance assignment based on optimal agreement between the experimental and calculated RDCs from a structural template that...
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[NMR paper] NMR assignment of the turtle prion protein fragment tPrP(121-225).
NMR assignment of the turtle prion protein fragment tPrP(121-225).
Related Articles NMR assignment of the turtle prion protein fragment tPrP(121-225).
J Biomol NMR. 2004 Sep;30(1):97
Authors: Calzolai L, Lysek DA, Wüthrich K
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[NMR paper] PMP1 18-38, a yeast plasma membrane protein fragment, binds phosphatidylserine from b
PMP1 18-38, a yeast plasma membrane protein fragment, binds phosphatidylserine from bilayer mixtures with phosphatidylcholine: a (2)H-NMR study.
Related Articles PMP1 18-38, a yeast plasma membrane protein fragment, binds phosphatidylserine from bilayer mixtures with phosphatidylcholine: a (2)H-NMR study.
Biophys J. 2000 Nov;79(5):2624-31
Authors: Roux M, Beswick V, Coïc YM, Huynh-Dinh T, Sanson A, Neumann JM
PMP1 is a 38-residue plasma membrane protein of the yeast Saccharomyces cerevisiae that regulates the activity of the H(+)-ATPase. The...
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11-19-2010 08:29 PM
[NMR paper] Backbone dynamics of a bacterially expressed peptide from the receptor binding domain
Backbone dynamics of a bacterially expressed peptide from the receptor binding domain of Pseudomonas aeruginosa pilin strain PAK from heteronuclear 1H-15N NMR spectroscopy.
Related Articles Backbone dynamics of a bacterially expressed peptide from the receptor binding domain of Pseudomonas aeruginosa pilin strain PAK from heteronuclear 1H-15N NMR spectroscopy.
J Biomol NMR. 2000 Jul;17(3):239-55
Authors: Campbell AP, Spyracopoulos L, Irvin RT, Sykes BD
The backbone dynamics of a 15N-labeled recombinant PAK pilin peptide spanning residues...