REDCRAFT: A tool for simultaneous characterization of protein backbone structure and motion from RDC data

We report on the synthesis and detailed characterization of dendrimers that evolve symmetrically from a linear core of 2-butyne-1,4-diol with 3,5-dihydroxybenzyl alcohol based dendron arms. The divergent layer-by-layer build-up of the dumbbell-shaped dendrimers is based on simple acid–base hydrolytic chemistry of bis(dimethylamino)dimethylsilane with OH-terminated molecules. The self-assembly of these dendrimers in THF and water is significantly influenced by their generation number, the backbone structure, and the solvent.Key words: dendrimers, divergent synthesis, macromolecules, self-assembly

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Faculty Opinions recommendation of De novo determination of protein backbone structure from residual dipolar couplings using Rosetta.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.1006182.77113 ◽

2002 ◽

Author(s):

Kristina Downing

Keyword(s):

Residual Dipolar Couplings ◽

De Novo ◽

Dipolar Couplings ◽

Protein Backbone ◽

Backbone Structure

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Algorithms and Analytic Solutions Using Sparse Residual Dipolar Couplings for High-Resolution Automated Protein Backbone Structure Determination by NMR

Springer Tracts in Advanced Robotics - Algorithmic Foundations of Robotics IX ◽

10.1007/978-3-642-17452-0_21 ◽

2010 ◽

pp. 355-372 ◽

Cited By ~ 5

Author(s):

Anna Yershova ◽

Chittaranjan Tripathy ◽

Pei Zhou ◽

Bruce Randall Donald

Keyword(s):

High Resolution ◽

Structure Determination ◽

Residual Dipolar Couplings ◽

Analytic Solutions ◽

Dipolar Couplings ◽

Protein Backbone ◽

Backbone Structure

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Natural coordinate representation for the protein backbone structure

Proteins Structure Function and Bioinformatics ◽

10.1002/prot.10201 ◽

2002 ◽

Vol 49 (2) ◽

pp. 206-215 ◽

Cited By ~ 2

Author(s):

Cornelius G. Hunter ◽

Shankar Subramaniam

Keyword(s):

Protein Backbone ◽

Coordinate Representation ◽

Backbone Structure ◽

Natural Coordinate

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NMR Characterization of Side Chain Flexibility and Backbone Structure in the Type I Antifreeze Protein at Near Freezing Temperatures†

Biochemistry ◽

10.1021/bi961934w ◽

1996 ◽

Vol 35 (51) ◽

pp. 16698-16704 ◽

Cited By ~ 43

Author(s):

Wolfram Gronwald ◽

Heman Chao ◽

D. Venkat Reddy ◽

Peter L. Davies ◽

Brian D. Sykes ◽

...

Keyword(s):

Antifreeze Protein ◽

Side Chain ◽

Type I ◽

Chain Flexibility ◽

Nmr Characterization ◽

Backbone Structure ◽

Freezing Temperatures

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Structural and Genetic Characterization of Glycosylation of Type a Flagellin in Pseudomonas aeruginosa

Journal of Bacteriology ◽

10.1128/jb.186.9.2523-2531.2004 ◽

2004 ◽

Vol 186 (9) ◽

pp. 2523-2531 ◽

Cited By ~ 92

Author(s):

M. Schirm ◽

S. K. Arora ◽

A. Verma ◽

E. Vinogradov ◽

P. Thibault ◽

...

Keyword(s):

Pseudomonas Aeruginosa ◽

Gene Cluster ◽

Genetic Characterization ◽

Type A ◽

Protein Backbone ◽

Central Surface

ABSTRACT Type a flagellins from two strains of Pseudomonas aeruginosa, strains PAK and JJ692, were found to be glycosylated with unique glycan structures. In both cases, two sites of O-linked glycosylation were identified on each monomer, and these sites were localized to the central, surface-exposed domain of the monomer in the assembled filament. The PAK flagellin was modified with a heterogeneous glycan comprising up to 11 monosaccharide units that were O linked through a rhamnose residue to the protein backbone. The flagellin of JJ692 was less complex and had a single rhamnose substitution at each site. The role of the glycosylation island gene cluster in the production of each of these glycosyl moieties was investigated. These studies revealed that the orfA and orfN genes were required for attachment of the heterologous glycan and the proximal rhamnose residue, respectively.

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