Related Articles13C NMR study of the mode of interaction in solution of the B fragment of staphylococcal protein A and the Fc fragments of mouse immunoglobulin G.
FEBS Lett. 1993 Aug 9;328(1-2):49-54
Authors: Kato K, Gouda H, Takaha W, Yoshino A, Matsunaga C, Arata Y
The mode of interaction of the B domain (FB) of staphylococcal protein A and the Fc fragments of mouse immunoglobulin G (IgG) has been investigated by 13C NMR spectroscopy. Mouse IgG1, IgG2a, and IgG2b proteins have been selectively labeled with 13C at the carbonyl carbon of His, Met, Trp or Tyr residue and used to prepare the corresponding Fc fragments by limited proteolysis. Site-specific resonance assignments have been made for each of these Fc analogues. FB was reported to form two contacts (contact 1 and contact 2) with human Fc in the crystal [Biochemistry 20 (1981) 2361-2370]. Comparisons of the chemical shift data of the Fc fragments observed in the absence and presence of FB have led us to conclude that in solution contact 1 is responsible for the formation of the Fc-FB complexes.
Solid-state and unilateral NMR study of deterioration of a Dead Sea Scroll fragment.
Solid-state and unilateral NMR study of deterioration of a Dead Sea Scroll fragment.
Solid-state and unilateral NMR study of deterioration of a Dead Sea Scroll fragment.
Anal Bioanal Chem. 2011 Jul 30;
Authors: Masic A, Chierotti MR, Gobetto R, Martra G, Rabin I, Coluccia S
Unilateral and solid-state nuclear magnetic resonance (NMR) analyses were performed on a parchment fragment of the Dead Sea Scroll (DSS). The analyzed sample belongs to the collection of non-inscribed and nontreated fragments of known archaeological provenance from the John...
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[NMR paper] A REDOR NMR study of a phosphorylated statherin fragment bound to hydroxyapatite crystals.
A REDOR NMR study of a phosphorylated statherin fragment bound to hydroxyapatite crystals.
Related Articles A REDOR NMR study of a phosphorylated statherin fragment bound to hydroxyapatite crystals.
J Am Chem Soc. 2005 Jul 6;127(26):9350-1
Authors: Gibson JM, Raghunathan V, Popham JM, Stayton PS, Drobny GP
Hydroxyapatite (HAP) is the main mineral component of teeth. It is well-known that several salivary proteins and peptides bind strongly to HAP to regulate crystal growth. Interactions between a peptide derived from the N-terminal fragment of...
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[NMR paper] NMR fragment screening: tackling protein-protein interaction targets.
NMR fragment screening: tackling protein-protein interaction targets.
Related Articles NMR fragment screening: tackling protein-protein interaction targets.
Curr Opin Drug Discov Devel. 2005 May;8(3):365-73
Authors: Schade M, Oschkinat H
High-throughput screening of libraries containing compounds of 'drug-like' molecular weight has frequently resulted in no or poor drug candidates, especially when screening against demanding drug targets such as protein-protein interactions. Fragment-based lead discovery and optimization has evolved as a...
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[NMR paper] Determination of solution conformations of PrP106-126, a neurotoxic fragment of prion
Determination of solution conformations of PrP106-126, a neurotoxic fragment of prion protein, by 1H NMR and restrained molecular dynamics.
Related Articles Determination of solution conformations of PrP106-126, a neurotoxic fragment of prion protein, by 1H NMR and restrained molecular dynamics.
Eur J Biochem. 1999 Dec;266(3):1192-201
Authors: Ragg E, Tagliavini F, Malesani P, Monticelli L, Bugiani O, Forloni G, Salmona M
Experimental two-dimensional 1H NMR data have been obtained for PrP106-128 under the following solvent conditions:...
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11-18-2010 08:31 PM
[NMR paper] NMR solution structure of the 205-316 C-terminal fragment of thermolysin. An example
NMR solution structure of the 205-316 C-terminal fragment of thermolysin. An example of dimerization coupled to partial unfolding.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles NMR solution structure of the 205-316 C-terminal fragment of thermolysin. An example of dimerization coupled to partial unfolding.
Biochemistry. 1997 Sep 30;36(39):11975-83
Authors: Conejero-Lara F, González C, Jiménez MA, Padmanabhan S, Mateo PL, Rico M
The solution structure of the C-terminal fragment...
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[NMR paper] Elucidation of the primary structure of the lantibiotic epilancin K7 from Staphylococ
Elucidation of the primary structure of the lantibiotic epilancin K7 from Staphylococcus epidermidis K7. Cloning and characterisation of the epilancin-K7-encoding gene and NMR analysis of mature epilancin K7.
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 Elucidation of the primary structure of the lantibiotic epilancin K7 from Staphylococcus epidermidis K7. Cloning and characterisation of the epilancin-K7-encoding gene and NMR analysis of mature epilancin K7.
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[NMR paper] NMR study of the reconstitution of the beta-sheet of thioredoxin by fragment compleme
NMR study of the reconstitution of the beta-sheet of thioredoxin by fragment complementation.
Related Articles NMR study of the reconstitution of the beta-sheet of thioredoxin by fragment complementation.
Proteins. 1995 May;22(1):41-4
Authors: Tasayco ML, Chao K
The study of complementary protein fragments is thought to be generally useful to identify early folding intermediates. A prerequisite for these studies is the reconstitution of the native-like structure by fragment complementation. Structural analysis of the complementation of the...
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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...
13C NMR study of the mode of interaction in solution of the B fragment of staphylococ
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