In nature, proteins are organized into highly ordered self-assembled structures with various morphologies and dimensions. In their Communication (DOI: 10.1002/anie.201703052), Y. Ma, G. Chen, and co-workers report the fabrication of protein assemblies by using native protein LecA as a building block through sugar–protein interactions and rhodamine dimerization. The morphologies and dimensions of the protein assemblies can be controlled by the length of the tether between the sugar and rhodamine.
Molecular Dissection of the Forces Responsible forViral Capsid Assembly and Stabilization by Decoration Proteins
Molecular Dissection of the Forces Responsible forViral Capsid Assembly and Stabilization by Decoration Proteins
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.6b00705/20170125/images/medium/bi-2016-00705u_0008.gif
Biochemistry
DOI: 10.1021/acs.biochem.6b00705
http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/bichaw/~4/j9Ibvk-KE98
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01-25-2017 11:13 PM
[NMR paper] Tangled web of interactions among proteins involved in iron-sulfur cluster assembly as unraveled by NMR, SAXS, chemical crosslinking, and functional studies.
Tangled web of interactions among proteins involved in iron-sulfur cluster assembly as unraveled by NMR, SAXS, chemical crosslinking, and functional studies.
Tangled web of interactions among proteins involved in iron-sulfur cluster assembly as unraveled by NMR, SAXS, chemical crosslinking, and functional studies.
Biochim Biophys Acta. 2014 Nov 22;
Authors: Kim JH, Bothe JR, Reid Alderson T, Markley JL
Abstract
Proteins containing iron-sulfur (Fe-S) clusters arose early in evolution and are essential to life. Organisms have...
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12-03-2014 04:05 PM
Tangled web of interactions among proteins involved in iron-sulfur cluster assembly as unraveled by NMR, SAXS, chemical crosslinking, and functional studies
Tangled web of interactions among proteins involved in iron-sulfur cluster assembly as unraveled by NMR, SAXS, chemical crosslinking, and functional studies
Publication date: Available online 22 November 2014
Source:Biochimica et Biophysica Acta (BBA) - Molecular Cell Research</br>
Author(s): Jin Hae Kim , Jameson R. Bothe , T. Reid Alderson , John L. Markley</br>
Proteins containing iron-sulfur (Fe-S) clusters arose early in evolution and are essential to life. Organisms have evolved machinery consisting of specialized proteins that operate together to assemble...
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11-22-2014 01:48 PM
An improved algorithm for MFR fragment assembly
An improved algorithm for MFR fragment assembly
Abstract A method for generating protein backbone models from backbone only NMR data is presented, which is based on molecular fragment replacement (MFR). In a first step, the PDB database is mined for homologous peptide fragments using experimental backbone-only data i.e. backbone chemical shifts (CS) and residual dipolar couplings (RDC). Second, this fragment library is refined against the experimental restraints. Finally, the fragments are assembled into a protein backbone fold using a rigid body docking algorithm using the RDCs as...
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05-17-2012 08:40 AM
Solution NMR structure of Dsy0195 homodimer from Desulfitobacterium hafniense: first structure representative of the YabP domain family of proteins involved in spore coat assembly.
Solution NMR structure of Dsy0195 homodimer from Desulfitobacterium hafniense: first structure representative of the YabP domain family of proteins involved in spore coat assembly.
Solution NMR structure of Dsy0195 homodimer from Desulfitobacterium hafniense: first structure representative of the YabP domain family of proteins involved in spore coat assembly.
J Struct Funct Genomics. 2011 Sep 9;
Authors: Yang Y, Ramelot TA, Cort JR, Wang H, Ciccosanti C, Jiang M, Janjua H, Acton TB, Xiao R, Everett JK, Montelione GT, Kennedy MA
Abstract
...
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09-10-2011 06:51 PM
Free-Standing Mesoporous Carbon Thin Films with Highly Ordered Pore Architectures for Nanodevices
Free-Standing Mesoporous Carbon Thin Films with Highly Ordered Pore Architectures for Nanodevices
Dan Feng, Yingying Lv, Zhangxiong Wu, Yuqian Dou, Lu Han, Zhenkun Sun, Yongyao Xia, Gengfeng Zheng and Dongyuan Zhao
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja2056227/aop/images/medium/ja-2011-056227_0008.gif
Journal of the American Chemical Society
DOI: 10.1021/ja2056227
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/kH5IriZSWVA
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09-07-2011 08:21 AM
Exploring collagen self-assembly by NMR.
Exploring collagen self-assembly by NMR.
Related Articles Exploring collagen self-assembly by NMR.
Phys Chem Chem Phys. 2010 Sep 28;
Authors: Lisitza N, Huang X, Hatabu H, Patz S
The time-dependence of the NMR signal intensity of collagen type I is representative of protein aggregation. It is pH sensitive and can be related to aggregation mechanism.
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09-30-2010 06:54 PM
[CNS Yahoo group] PDBePISA assembly, summary and XML data files available from the Pro
PDBePISA assembly, summary and XML data files available from the Pro
The Protein Data Bank in Europe (PDBe; http://pdbe.org/) is pleased to announce the availability of PISA assembly files, summaries and associated XML
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Highly Ordered Self-Assembly of Native Proteins into 1D, 2D, and 3D Structures Modulated by the Tether Length of Assembly-Inducing Ligands
Linear Mode
