It has been shown that human seminal fluid is a major factor in enhancing HIV activity. The SEM2(49-107) peptide is a product of cleavage after ejaculation by internal prostheses of the semenogelin 2 protein, expressed in seminal vesicles. It is established that the peptide SEM2(49-107) forms amyloid fibrils, which increase probability of contracting HIV infection. In this nuclear magnetic resonance (NMR) study, we present almost complete (86%) resonance assignments for the ¹H ^(15)N and ^(13)C...
[NMR paper] NMR resonance assignments for a docking domain pair with an attached thiolation domain from the PAX peptide-producing NRPS from Xenorhabdus cabanillasii
NMR resonance assignments for a docking domain pair with an attached thiolation domain from the PAX peptide-producing NRPS from Xenorhabdus cabanillasii
Non-ribosomal peptide synthetases (NRPSs) are large multienzyme machineries. They synthesize numerous important natural products starting from amino acids. For peptide synthesis functionally specialized NRPS modules interact in a defined manner. Individual modules are either located on a single or on multiple different polypeptide chains. The "peptide-antimicrobial-Xenorhabdus" (PAX) peptide producing NRPS PaxS from Xenorhabdus bacteria...
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03-07-2021 07:38 AM
[NMR paper] Membrane remodeling by amyloidogenic and non-amyloidogenic proteins studied by EPR
Membrane remodeling by amyloidogenic and non-amyloidogenic proteins studied by EPR
Publication date: July 2017
Source:Journal of Magnetic Resonance, Volume 280</br>
Author(s): Jobin Varkey, Ralf Langen</br>
The advancement in site-directed spin labeling of proteins has enabled EPR studies to expand into newer research areas within the umbrella of protein-membrane interactions. Recently, membrane remodeling by amyloidogenic and non-amyloidogenic proteins has gained a substantial interest in relation to driving and controlling vital cellular processes such as...
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06-02-2017 08:33 PM
[NMR paper] Specific binding of a naturally occurring amyloidogenic fragment of Streptococcus mutans adhesin P1 to intact P1 on the cell surface characterized by solid state NMR spectroscopy.
Specific binding of a naturally occurring amyloidogenic fragment of Streptococcus mutans adhesin P1 to intact P1 on the cell surface characterized by solid state NMR spectroscopy.
Specific binding of a naturally occurring amyloidogenic fragment of Streptococcus mutans adhesin P1 to intact P1 on the cell surface characterized by solid state NMR spectroscopy.
J Biomol NMR. 2016 Feb 2;
Authors: Tang W, Bhatt A, Smith AN, Crowley PJ, Brady LJ, Long JR
Abstract
The P1 adhesin (aka Antigen I/II or PAc) of the cariogenic bacterium...
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02-04-2016 11:46 AM
Specific binding of a naturally occurring amyloidogenic fragment of Streptococcus mutans adhesin P1 to intact P1 on the cell surface characterized by solid state NMR spectroscopy
Specific binding of a naturally occurring amyloidogenic fragment of Streptococcus mutans adhesin P1 to intact P1 on the cell surface characterized by solid state NMR spectroscopy
Abstract
The P1 adhesin (aka Antigen I/II or PAc) of the cariogenic bacterium Streptococcus mutans is a cell surface-localized protein involved in sucrose-independent adhesion and colonization of the tooth surface. The immunoreactive and adhesive properties of S. mutans suggest an unusual functional quaternary ultrastructure comprised of intact P1 covalently attached to the...
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02-02-2016 08:58 PM
[NMR paper] NMR resonance assignments of the catalytic domain of human serine/threonine phosphatase calcineurin in unligated and PVIVIT-peptide-bound states.
NMR resonance assignments of the catalytic domain of human serine/threonine phosphatase calcineurin in unligated and PVIVIT-peptide-bound states.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles NMR resonance assignments of the catalytic domain of human serine/threonine phosphatase calcineurin in unligated and PVIVIT-peptide-bound states.
Biomol NMR Assign. 2015 Apr;9(1):201-5
Authors: Takeuchi K, Sun ZY, Li S, Gal M, Wagner G
Abstract
...
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11-14-2015 03:37 PM
[NMR paper] Bacterial expression and purification of the amyloidogenic peptide PAPf39 for multidimensional NMR spectroscopy.
Bacterial expression and purification of the amyloidogenic peptide PAPf39 for multidimensional NMR spectroscopy.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Bacterial expression and purification of the amyloidogenic peptide PAPf39 for multidimensional NMR spectroscopy.
Protein Expr Purif. 2013 Apr;88(2):196-200
Authors: Shanmuganathan A, Bishop AC, French KC, McCallum SA, Makhatadze GI
Abstract
PAPf39 is a 39 residue peptide fragment from human...
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08-23-2013 01:07 AM
[NMR paper] Resonance assignments and secondary structure analysis of E. coli thioredoxin by magic angle spinning solid-state NMR spectroscopy.
Resonance assignments and secondary structure analysis of E. coli thioredoxin by magic angle spinning solid-state NMR spectroscopy.
Related Articles Resonance assignments and secondary structure analysis of E. coli thioredoxin by magic angle spinning solid-state NMR spectroscopy.
J Phys Chem B. 2005 Sep 29;109(38):18135-45
Authors: Marulanda D, Tasayco ML, Cataldi M, Arriaran V, Polenova T
De novo site-specific 13C and 15N backbone and sidechain resonance assignments are presented for uniformly enriched E. coli thioredoxin, established using...
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12-01-2010 06:56 PM
NMR chemical shift assignments of a complex between SUMO-1 and SIM peptide derived fr
NMR chemical shift assignments of a complex between SUMO-1 and SIM peptide derived from the C-terminus of Daxx.
Related Articles NMR chemical shift assignments of a complex between SUMO-1 and SIM peptide derived from the C-terminus of Daxx.
Biomol NMR Assign. 2010 Oct 7;
Authors: Naik MT, Chang CC, Naik NM, Kung CC, Shih HM, Huang TH
Small Ubiquitin-like MOdifiers (SUMOs) are ubiquitin-like proteins known to covalently modify large number of cellular proteins. The mammalian SUMO family includes four paralogues, SUMO-1 through SUMO-4....