Tissue Inhibitor of Metalloprotease-2 (TIMP-2):Bioprocess Development, Physicochemical, Biochemical, and BiologicalCharacterization of Highly Expressed Recombinant Protein
Tissue Inhibitor of Metalloprotease-2 (TIMP-2):Bioprocess Development, Physicochemical, Biochemical, and BiologicalCharacterization of Highly Expressed Recombinant Protein
[NMR paper] Recombinant expression of Ixolaris, a Kunitz-type inhibitor from the tick salivary gland, for NMR studies.
Recombinant expression of Ixolaris, a Kunitz-type inhibitor from the tick salivary gland, for NMR studies.
Related Articles Recombinant expression of Ixolaris, a Kunitz-type inhibitor from the tick salivary gland, for NMR studies.
Protein Expr Purif. 2017 Jul 19;:
Authors: De Paula VS, Silva FHS, Francischetti IMB, Monteiro RQ, Valente AP
Abstract
Ixolaris is an anticoagulant protein identified in the tick saliva of Ixodes scapularis. Ixolaris contains 2 Kunitz like domains and binds to Factor Xa or Factor X as a scaffold for...
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07-24-2017 10:10 AM
[NMR paper] Structure and pharmaceutical formulation development of a new long-acting recombinant human insulin analog studied by NMR and MS.
Structure and pharmaceutical formulation development of a new long-acting recombinant human insulin analog studied by NMR and MS.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Structure and pharmaceutical formulation development of a new long-acting recombinant human insulin analog studied by NMR and MS.
J Pharm Biomed Anal. 2017 Feb 20;135:126-132
Authors: Bednarek E, Sitkowski J, Bocian W, Borowicz P, P?ucienniczak G, Stadnik D, Surmacz-Chwedoruk W,...
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05-26-2017 08:36 PM
Bacterial production of site specific 13 C labeled phenylalanine and methodology for high level incorporation into bacterially expressed recombinant proteins
Bacterial production of site specific 13 C labeled phenylalanine and methodology for high level incorporation into bacterially expressed recombinant proteins
Abstract
Nuclear magnetic resonance spectroscopy studies of ever larger systems have benefited from many different forms of isotope labeling, in particular, site specific isotopic labeling. Site specific 13C labeling of methyl groups has become an established means of probing systems not amenable to traditional methodology. However useful, methyl reporter sites can be limited in number and/or...
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12-27-2016 11:04 PM
[NMR paper] A novel 2-oxoindolinylidene inhibitor of bacterial MurD ligase: Enzyme kinetics, protein-inhibitor binding by NMR and a molecular dynamics study.
A novel 2-oxoindolinylidene inhibitor of bacterial MurD ligase: Enzyme kinetics, protein-inhibitor binding by NMR and a molecular dynamics study.
Related Articles A novel 2-oxoindolinylidene inhibitor of bacterial MurD ligase: Enzyme kinetics, protein-inhibitor binding by NMR and a molecular dynamics study.
Eur J Med Chem. 2014 Jun 11;83C:92-101
Authors: Sim?i? M, Pureber K, Kristan K, Urleb U, Kocjan D, Grdadolnik SG
Abstract
N-(5-(5-nitro-2-oxo-1,2-dihydro-3H-indol-3-ylidene)4-oxo-2-thioxo-1,3-thiazolidin-3-yl)nicotinamide,...
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06-22-2014 12:24 PM
A Novel 2-oxoindolinylidene Inhibitor of Bacterial MurD Ligase: Enzyme Kinetics, Protein-Inhibitor Binding by NMR and a Molecular Dynamics Study
A Novel 2-oxoindolinylidene Inhibitor of Bacterial MurD Ligase: Enzyme Kinetics, Protein-Inhibitor Binding by NMR and a Molecular Dynamics Study
Publication date: Available online 11 June 2014
Source:European Journal of Medicinal Chemistry</br>
Author(s): Mihael Sim?i? , Kaja Pureber , Katja Kristan , Uro Urleb , Darko Kocjan , Simona Goli? Grdadolnik</br>
N-(5-(5-nitro-2-oxo-1,2-dihydro-3H-indol-3-ylidene)4-oxo-2-thioxo-1,3-thiazolidin-3-yl)nicotinamide, an 2-oxoindolinylidene derivative with novel structure scaffold, was evaluated for inhibition potency...
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06-12-2014 10:52 PM
Segmental isotopic labeling of a 140 kDa dimeric multi-domain protein CheA from Escherichia coli by expressed protein ligation and protein trans-splicing
Segmental isotopic labeling of a 140 kDa dimeric multi-domain protein CheA from Escherichia coli by expressed protein ligation and protein trans-splicing
Abstract Segmental isotopic labeling is a powerful labeling tool to facilitate NMR studies of larger proteins by not only alleviating the signal overlap problem but also retaining features of uniform isotopic labeling. Although two approaches, expressed protein ligation (EPL) and protein trans-splicing (PTS), have been mainly used for segmental isotopic labeling, there has been no single example in which both approaches have been...
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07-02-2012 06:18 AM
NMR structure and dynamics of recombinant wild type and mutated jerdostatin, a selective inhibitor of integrin ?(1) ?(1).
NMR structure and dynamics of recombinant wild type and mutated jerdostatin, a selective inhibitor of integrin ?(1) ?(1).
NMR structure and dynamics of recombinant wild type and mutated jerdostatin, a selective inhibitor of integrin ?(1) ?(1).
Proteins. 2011 May 10;
Authors: Carbajo RJ, Sanz L, Mosulén S, Pérez A, Marcinkiewicz C, Pineda-Lucena A, Calvete JJ
NMR analysis of four recombinant jerdostatin molecules was assessed to define the structural basis of two naturally occurring gain-of-function events: C-terminal dipeptide processing and...
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06-10-2011 11:52 AM
[NMR paper] TIMP-1 contact sites and perturbations of stromelysin 1 mapped by NMR and a paramagne
TIMP-1 contact sites and perturbations of stromelysin 1 mapped by NMR and a paramagnetic surface probe.
Related Articles TIMP-1 contact sites and perturbations of stromelysin 1 mapped by NMR and a paramagnetic surface probe.
Biochemistry. 1998 Jul 7;37(27):9650-7
Authors: Arumugam S, Hemme CL, Yoshida N, Suzuki K, Nagase H, Berjanskii M, Wu B, Van Doren SR
Surfaces of the 173 residue catalytic domain of human matrix metalloproteinase 3 (MMP-3(DeltaC)) affected by binding of the N-terminal, 126 residue inhibitory domain of human TIMP-1...
Tissue Inhibitor of Metalloprotease-2 (TIMP-2):Bioprocess Development, Physicochemical, Biochemical, and BiologicalCharacterization of Highly Expressed Recombinant Protein
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