[NMR paper] 6-Strand to Stable 10/12 Helix Conformational Switch by Incorporating Flexible beta-hGly in the Homooligomers of Camphor Derived beta-Amino Acid: NMR and X-ray Crystallographic Evidence
6-Strand to Stable 10/12 Helix Conformational Switch by Incorporating Flexible beta-hGly in the Homooligomers of Camphor Derived beta-Amino Acid: NMR and X-ray Crystallographic Evidence
Rational design of unnatural amino acid building blocks capable of stabilizing predictable secondary structures similar to protein fragments is pivotal for foldamer chemistry/catalysis. Here, we introduce novel ?-amino acid building blocks: [1S,2R,4R]exoCDA and [1S,2S,4R]endoCDA, derived from the abundantly available R(+)-camphor, which is traditionally known for its medicinal value. Further, we demonstrate that the homooligomers of exoCDA adopt 6-strand conformation, which switches to a robust...
Analysis of {beta}2AR-Gs and {beta}2AR-Gi complex formation by NMR spectroscopy [Pharmacology]
Analysis of {beta}2AR-Gs and {beta}2AR-Gi complex formation by NMR spectroscopy
Xiuyan Ma, Yunfei Hu, Hossein Batebi, Jie Heng, Jun Xu, Xiangyu Liu, Xiaogang Niu, Hongwei Li, Peter W. Hildebrand, Changwen Jin, Brian K. Kobilka...
Date: 2020-09-15
The ?2-adrenergic receptor (?2AR) is a prototypical G protein-coupled receptor (GPCR) that preferentially couples to the stimulatory G protein Gs and stimulates cAMP formation. Functional studies have shown that the ?2AR also couples to inhibitory G protein Gi, activation of which inhibits cAMP formation Read More
PNAS:
Number: 37
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[NMR paper] NMR Analysis of Tuning Cross-Strand Phe/Tyr/Trp - Trp Interactions in Designed ?-Hairpin Peptides: Terminal Switch from L- to D-Amino Acid as a Strategy for ?-Hairpin Capping.
NMR Analysis of Tuning Cross-Strand Phe/Tyr/Trp - Trp Interactions in Designed ?-Hairpin Peptides: Terminal Switch from L- to D-Amino Acid as a Strategy for ?-Hairpin Capping.
Related Articles NMR Analysis of Tuning Cross-Strand Phe/Tyr/Trp - Trp Interactions in Designed ?-Hairpin Peptides: Terminal Switch from L- to D-Amino Acid as a Strategy for ?-Hairpin Capping.
J Phys Chem B. 2015 Apr 7;
Authors: Makwana KM, Mahalakshmi R
Abstract
Interaction among the side chains of aromatic amino acids is a well-known mechanism of protein...
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[NMR paper] The NMR structure of a stable and compact all-beta-sheet variant of intestinal fatty
The NMR structure of a stable and compact all-beta-sheet variant of intestinal fatty acid-binding protein.
Related Articles The NMR structure of a stable and compact all-beta-sheet variant of intestinal fatty acid-binding protein.
Protein Sci. 2004 May;13(5):1227-37
Authors: Ogbay B, Dekoster GT, Cistola DP
Intestinal fatty acid-binding protein (I-FABP) has a clam-shaped structure that may serve as a scaffold for the design of artificial enzymes and drug carriers. In an attempt to optimize the scaffold for increased access to the...
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[NMR paper] alpha-->beta transition of beta-lactoglobulin as evidenced by heteronuclear NMR.
alpha-->beta transition of beta-lactoglobulin as evidenced by heteronuclear NMR.
Related Articles alpha-->beta transition of beta-lactoglobulin as evidenced by heteronuclear NMR.
J Mol Biol. 1998 Nov 6;283(4):731-9
Authors: Kuwata K, Hoshino M, Era S, Batt CA, Goto Y
Whereas bovine beta-lactoglobulin is a predominantly beta-sheet protein, it has a marked alpha-helical preference and can be considered to be a useful model of the alpha-->beta transition, a key issue for understanding the folding and biological function of a number of proteins....
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[NMR paper] High helicity of peptide fragments corresponding to beta-strand regions of beta-lacto
High helicity of peptide fragments corresponding to beta-strand regions of beta-lactoglobulin observed by 2D-NMR spectroscopy.
Related Articles High helicity of peptide fragments corresponding to beta-strand regions of beta-lactoglobulin observed by 2D-NMR spectroscopy.
Fold Des. 1996;1(4):255-63
Authors: Kuroda Y, Hamada D, Tanaka T, Goto Y
BACKGROUND: Whereas protein fragments, when they are structured, adopt conformations similar to that found in the native state, the high helical propensity of beta-lactoglobulin, a predominantly beta-sheet...
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[NMR paper] Solution structure of rat apo-S100B(beta beta) as determined by NMR spectroscopy.
Solution structure of rat apo-S100B(beta beta) as determined by NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Solution structure of rat apo-S100B(beta beta) as determined by NMR spectroscopy.
Biochemistry. 1996 Sep 10;35(36):11577-88
Authors: Drohat AC, Amburgey JC, Abildgaard F, Starich MR, Baldisseri D, Weber DJ
S100B(beta beta), a member of the S100 protein family, is a Ca(2+)-binding protein with noncovalent interactions at its dimer interface. Each apo-S100 beta...
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[NMR paper] High-resolution solution structure of the beta chemokine hMIP-1 beta by multidimensio
High-resolution solution structure of the beta chemokine hMIP-1 beta by multidimensional NMR.
Related Articles High-resolution solution structure of the beta chemokine hMIP-1 beta by multidimensional NMR.
Science. 1994 Mar 25;263(5154):1762-7
Authors: Lodi PJ, Garrett DS, Kuszewski J, Tsang ML, Weatherbee JA, Leonard WJ, Gronenborn AM, Clore GM
The three-dimensional structure of a member of the beta subfamily of chemokines, human macrophage inflammatory protein-1 beta (hMIP-1 beta), has been determined with the use of solution multidimensional...
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[NMR paper] High-resolution solution structure of the beta chemokine hMIP-1 beta by multidimensio
High-resolution solution structure of the beta chemokine hMIP-1 beta by multidimensional NMR.
Related Articles High-resolution solution structure of the beta chemokine hMIP-1 beta by multidimensional NMR.
Science. 1994 Mar 25;263(5154):1762-7
Authors: Lodi PJ, Garrett DS, Kuszewski J, Tsang ML, Weatherbee JA, Leonard WJ, Gronenborn AM, Clore GM
The three-dimensional structure of a member of the beta subfamily of chemokines, human macrophage inflammatory protein-1 beta (hMIP-1 beta), has been determined with the use of solution multidimensional...