Related ArticlesNMR structure and functional characteristics of the hydrophilic N terminus of the potassium channel beta-subunit Kvbeta1.1.
J Biol Chem. 1999 Dec 10;274(50):35521-5
Authors: Wissmann R, Baukrowitz T, Kalbacher H, Kalbitzer HR, Ruppersberg JP, Pongs O, Antz C, Fakler B
Rapid N-type inactivation of voltage-dependent potassium (Kv) channels controls membrane excitability and signal propagation in central neurons and is mediated by protein domains (inactivation gates) occluding the open channel pore from the cytoplasmic side. Inactivation domains (ID) are donated either by the pore-forming alpha-subunit or certain auxiliary beta-subunits. Upon coexpression, Kvbeta1.1 was found to endow non-inactivating members of the Kv1alpha family with fast inactivation via its unique N terminus. Here we investigated structure and functional properties of the Kvbeta1.1 N terminus (amino acids 1-62, betaN-(1-62)) using NMR spectroscopy and patch clamp recordings. betaN-(1-62) showed all hallmarks of N-type inactivation: it inactivated non-inactivating Kv1.1 channels when applied to the cytoplasmic side as a synthetic peptide, and its interaction with the alpha-subunit was competed with tetraethylammonium and displayed an affinity in the lower micromolar range. In aequous and physiological salt solution, betaN-(1-62) showed no well defined three-dimensional structure, it rather existed in a fast equilibrium of multiple weakly structured states. These structural and functional properties of betaN-(1-62) closely resemble those of the "unstructured" ID from Shaker B, but differ markedly from those of the compactly folded ID of the Kv3.4 alpha-subunit.
[NMR paper] Solution NMR structure and folding dynamics of the N terminus of a rat non-muscle alp
Solution NMR structure and folding dynamics of the N terminus of a rat non-muscle alpha-tropomyosin in an engineered chimeric protein.
Related Articles Solution NMR structure and folding dynamics of the N terminus of a rat non-muscle alpha-tropomyosin in an engineered chimeric protein.
J Mol Biol. 2001 Sep 28;312(4):833-47
Authors: Greenfield NJ, Huang YJ, Palm T, Swapna GV, Monleon D, Montelione GT, Hitchcock-DeGregori SE
Tropomyosin is an alpha-helical coiled-coil protein that aligns head-to-tail along the length of the actin filament and...
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[NMR paper] NMR structure determination and structure-based functional characterization of conser
NMR structure determination and structure-based functional characterization of conserved hypothetical protein MTH1175 from Methanobacterium thermoautotrophicum.
Related Articles NMR structure determination and structure-based functional characterization of conserved hypothetical protein MTH1175 from Methanobacterium thermoautotrophicum.
J Struct Funct Genomics. 2000;1(1):15-25
Authors: Cort JR, Yee A, Edwards AM, Arrowsmith CH, Kennedy MA
The solution structure of MTH1175, a 124-residue protein from the archaeon Methanobacterium...
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[NMR paper] Protein-water interactions from 2H NMR relaxation studies: influence of hydrophilic,
Protein-water interactions from 2H NMR relaxation studies: influence of hydrophilic, hydrophobic, and electrostatic interactions.
Related Articles Protein-water interactions from 2H NMR relaxation studies: influence of hydrophilic, hydrophobic, and electrostatic interactions.
Adv Exp Med Biol. 1991;302:541-60
Authors: Kumosinski TF, Pessen H, Farrell HM
The importance of water interactions with proteins in food systems is well documented. A controversy exists, however, as to the nature of these interactions and the effect of protein structural...
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08-21-2010 11:16 PM
[NMR paper] Secondary and tertiary structure characteristics of Megasphaera elsdenii flavodoxin i
Secondary and tertiary structure characteristics of Megasphaera elsdenii flavodoxin in the reduced state as determined by two-dimensional 1H NMR.
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 Secondary and tertiary structure characteristics of Megasphaera elsdenii flavodoxin in the reduced state as determined by two-dimensional 1H NMR.
Eur J Biochem. 1990 May 20;189(3):589-600
Authors: van Mierlo CP, Müller F, Vervoort J
The...
[NMR paper] NMR structure and functional studies of the Mu repressor DNA-binding domain.
NMR structure and functional studies of the Mu repressor DNA-binding domain.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles NMR structure and functional studies of the Mu repressor DNA-binding domain.
Biochemistry. 1999 Jun 29;38(26):8367-76
Authors: Ilangovan U, Wojciak JM, Connolly KM, Clubb RT
The repressor protein of bacteriophage Mu establishes and maintains lysogeny by shutting down transposition functions needed for phage DNA replication. It interacts with several repeated DNA...
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[NMR paper] Solution structure of the carboxyl terminus of a human class Mu glutathione S-transfe
Solution structure of the carboxyl terminus of a human class Mu glutathione S-transferase: NMR assignment strategies in large proteins.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Solution structure of the carboxyl terminus of a human class Mu glutathione S-transferase: NMR assignment strategies in large proteins.
J Mol Biol. 1999 Feb 5;285(5):2119-32
Authors: McCallum SA, Hitchens TK, Rule GS
Strategies to obtain the NMR assignments for the HN, N, CO, Calpha and...
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Robust structure-based resonance assignment for functional protein studies by NMR
Abstract High-throughput functional protein NMR studies, like protein interactions or dynamics, require an automated approach for the assignment of the protein backbone. With the availability of a growing number of protein 3D structures, a new class of automated approaches, called structure-based assignment, has been developed quite recently. Structure-based approaches use primarily NMR input data that are not based on J-coupling and for which connections between residues are not limited by through bonds magnetization transfer efficiency. We present here a robust structure-based assignment...
NMR structure and functional characteristics of the hydrophilic N terminus of the pot
Linear Mode
