Cytoplasmic dynein complexes play crucial roles in intracellular transport of cellular organelles. While the motor domain of dynein is well characterized by techniques such as X-ray crystallography and cryo-electron microscopy (Cryo-EM), structural representations of dynein usually include only the more packed and easily resolved regions and omit the long flexible and poorly structured regions. One such flexible region is the N-terminal half of the intermediate chain (IC), which contains almost...
[NMR paper] Conformational Plasticity of the Cell-Penetrating Peptide SAP As Revealed by Solid-State 19F-NMR and Circular Dichroism Spectroscopies.
Conformational Plasticity of the Cell-Penetrating Peptide SAP As Revealed by Solid-State 19F-NMR and Circular Dichroism Spectroscopies.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles Conformational Plasticity of the Cell-Penetrating Peptide SAP As Revealed by Solid-State 19F-NMR and Circular Dichroism Spectroscopies.
J Phys Chem B. 2017 07 13;121(27):6479-6491
Authors: Afonin S, Kubyshkin V, Mykhailiuk PK, Komarov IV, Ulrich AS
Abstract
The...
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[NMR paper] Conformational plasticity of the NNRTI-binding pocket in HIV-1 reverse transcriptase - A fluorine NMR study.
Conformational plasticity of the NNRTI-binding pocket in HIV-1 reverse transcriptase - A fluorine NMR study.
Related Articles Conformational plasticity of the NNRTI-binding pocket in HIV-1 reverse transcriptase - A fluorine NMR study.
Biochemistry. 2016 May 10;
Authors: Sharaf NG, Ishima R, Gronenborn AM
Abstract
HIV-1 reverse transcriptase (RT) is a major drug target in the treatment of HIV-1 infection. RT inhibitors currently in use include non-nucleoside, allosteric RT inhibitors (NNRTIs), which bind to a hydrophobic pocket,...
Unravelling the Conformational Plasticity of the Extracellular Domain of a Prokaryotic nAChR Homologue in Solution by NMR
Unravelling the Conformational Plasticity of the Extracellular Domain of a Prokaryotic nAChR Homologue in Solution by NMR
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/bi201223u/aop/images/medium/bi-2011-01223u_0002.gif
Biochemistry
DOI: 10.1021/bi201223u
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[NMR paper] Local structural plasticity of the prion protein. Analysis of NMR relaxation dynamics
Local structural plasticity of the prion protein. Analysis of NMR relaxation dynamics.
Related Articles Local structural plasticity of the prion protein. Analysis of NMR relaxation dynamics.
Biochemistry. 2001 Mar 6;40(9):2743-53
Authors: Viles JH, Donne D, Kroon G, Prusiner SB, Cohen FE, Dyson HJ, Wright PE
A template-assisted conformational change of the cellular prion protein (PrP(C)) from a predominantly helical structure to an amyloid-type structure with a higher proportion of beta-sheet is thought to be the causative factor in prion...
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[NMR paper] NMR analysis of main-chain conformational preferences in an unfolded fibronectin-bind
NMR analysis of main-chain conformational preferences in an unfolded fibronectin-binding protein.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles NMR analysis of main-chain conformational preferences in an unfolded fibronectin-binding protein.
J Mol Biol. 1997 Nov 28;274(2):152-9
Authors: Penkett CJ, Redfield C, Dodd I, Hubbard J, McBay DL, Mossakowska DE, Smith RA, Dobson CM, Smith LJ
A 130-residue fragment of the Staphylococcus aureus fibronectin-binding protein has...
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[NMR paper] Analysis of side-chain conformational distributions in neutrophil peptide-5 NMR struc
Analysis of side-chain conformational distributions in neutrophil peptide-5 NMR structures.
Related Articles Analysis of side-chain conformational distributions in neutrophil peptide-5 NMR structures.
Biopolymers. 1990 Dec;29(14):1807-22
Authors: Kominos D, Bassolino DA, Levy RM, Pardi A
The side-chain conformations have been analyzed in the antimicrobial peptide, Neutrophil Peptide-5 (NP-5), whose structure was independently generated from nmr-derived distance constraints using a distance geometry algorithm. The side-chain and peptide...