Structural and Functional Investigation of the Ag+/Cu+ Binding Domains of the Periplasmic AdaptorProtein SilB from Cupriavidus metallidurans CH34
Structural and Functional Investigation of the Ag+/Cu+ Binding Domains of the Periplasmic AdaptorProtein SilB from Cupriavidus metallidurans CH34
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.6b00022/20160513/images/medium/bi-2016-000226_0007.gif
Biochemistry
DOI: 10.1021/acs.biochem.6b00022
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nmrlearner
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05-15-2016 05:00 AM
Comparison of backbone dynamics of the type III antifreeze protein and antifreeze-like domain of human sialic acid synthase
Comparison of backbone dynamics of the type III antifreeze protein and antifreeze-like domain of human sialic acid synthase
Abstract
Antifreeze proteins (AFPs) are found in a variety of cold-adapted (psychrophilic) organisms to promote survival at subzero temperatures by binding to ice crystals and decreasing the freezing temperature of body fluids. The type III AFPs are small globular proteins that consist of one α-helix, three 310-helices, and two β-strands. Sialic acids play important roles in a variety of biological functions, such as...
nmrlearner
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01-09-2015 03:58 PM
Bacterial expression, purification, and model membrane reconstitution of the transmembrane and cytoplasmic domains of the human APP binding protein LR11/SorLA for NMR studies.
Bacterial expression, purification, and model membrane reconstitution of the transmembrane and cytoplasmic domains of the human APP binding protein LR11/SorLA for NMR studies.
Bacterial expression, purification, and model membrane reconstitution of the transmembrane and cytoplasmic domains of the human APP binding protein LR11/SorLA for NMR studies.
Protein Expr Purif. 2011 Feb 11;
Authors: Wang X, Gill Jr RL, Zhu Q, Tian F
LR11 (SorLA) is a recently identified neuronal protein that interacts with amyloid precursor protein (APP), a central player...
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02-16-2011 07:40 PM
NMR characterizations of the ice binding surface of an antifreeze protein.
NMR characterizations of the ice binding surface of an antifreeze protein.
NMR characterizations of the ice binding surface of an antifreeze protein.
PLoS One. 2010;5(12):e15682
Authors: Hong J, Hu Y, Li C, Jia Z, Xia B, Jin C
Antifreeze protein (AFP) has a unique function of reducing solution freezing temperature to protect organisms from ice damage. However, its functional mechanism is not well understood. An intriguing question concerning AFP function is how the high selectivity for ice ligand is achieved in the presence of free water of...
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01-07-2011 11:21 PM
[NMR paper] Hydrogen bonding on the ice-binding face of a beta-helical antifreeze protein indicat
Hydrogen bonding on the ice-binding face of a beta-helical antifreeze protein indicated by amide proton NMR chemical shifts.
Related Articles Hydrogen bonding on the ice-binding face of a beta-helical antifreeze protein indicated by amide proton NMR chemical shifts.
Biochemistry. 2004 Oct 19;43(41):13012-7
Authors: Daley ME, Graether SP, Sykes BD
The dependence of amide proton chemical shifts on temperature is used as an indication of the hydrogen bonding properties in a protein. The amide proton temperature coefficients of the beta-helical...
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11-24-2010 10:01 PM
[NMR paper] Energetics by NMR: site-specific binding in a positively cooperative system.
Energetics by NMR: site-specific binding in a positively cooperative system.
Related Articles Energetics by NMR: site-specific binding in a positively cooperative system.
Proc Natl Acad Sci U S A. 2002 Feb 19;99(4):1847-52
Authors: Tochtrop GP, Richter K, Tang C, Toner JJ, Covey DF, Cistola DP
Proteins with multiple binding sites exhibit a complex behavior that depends on the intrinsic affinities for each site and the energetic communication between the sites. The contributions from intrinsic affinity and cooperativity are difficult to...
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11-24-2010 08:49 PM
[NMR paper] NMR analysis of the hydrogen bonding interactions of the RNA-binding domains of the D
NMR analysis of the hydrogen bonding interactions of the RNA-binding domains of the Drosophila sex-lethal protein with target RNA fragments with site-specific uridine substitutions.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-custom-oxfordjournals_final_free.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles NMR analysis of the hydrogen bonding interactions of the RNA-binding domains of the Drosophila sex-lethal protein with...
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08-22-2010 03:31 PM
[NMR paper] NMR analysis of the hydrogen bonding interactions of the RNA-binding domains of the D
NMR analysis of the hydrogen bonding interactions of the RNA-binding domains of the Drosophila sex-lethal protein with target RNA fragments with site-specific uridine substitutions.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-custom-oxfordjournals_final_free.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles NMR analysis of the hydrogen bonding interactions of the RNA-binding domains of the Drosophila sex-lethal protein with...
Functional Analysis of a Bacterial Antifreeze Protein Indicates a Cooperative Effect between Its Two Ice-Binding Domains
Linear Mode
