To help understand the structure/function relationships in antifreeze proteins (AFP), and to define the motifs required for ice binding, a Type III AFP suitable for two-dimensional (2D) NMR studies was produced in Escherichia coli. A synthetic gene for one of the Type III AFP isoforms was assembled in a T7 polymerase-directed expression vector. The 67-amino acid-long gene product differed from the natural AFP by inclusion of an N-terminal methionine but was indistinguishable in activity. The NMR spectra of this AFP were complicated by cis-trans proline isomerization from the C-terminal sequence YPPA. Substitution of this sequence by YAA eliminated isomer signals without altering the activity or structure of the mutant AFP. This variant (rQAE m1.1) was selected for sequential assignment and the secondary structure determination using 2D 1H NMR spectroscopy. Nine beta-strands are paired to form two triple-stranded antiparallel sheets and one double-stranded antiparallel sheet. Two further proline replacements, P29A and P33A, were made to delineate the role of conserved prolines in Type III AFP. These mutants were valuable in clarifying ambiguous NMR spectral assignments amongst the remaining six prolines of rQAE m1.1. In contrast to the replacement of the C-terminal prolyl residues, the exchange of P29 and P33 caused some structural changes and significantly decreased protein solubility and antifreeze activity.
Metabolic relationship between polyhydroxyalkanoic acid and rhamnolipid synthesis in Pseudomonas aeruginosa: comparative 像C NMR analysis of the products in wild-type and mutants.
Metabolic relationship between polyhydroxyalkanoic acid and rhamnolipid synthesis in Pseudomonas aeruginosa: comparative 像C NMR analysis of the products in wild-type and mutants.
Metabolic relationship between polyhydroxyalkanoic acid and rhamnolipid synthesis in Pseudomonas aeruginosa: comparative 像C NMR analysis of the products in wild-type and mutants.
J Biotechnol. 2011 Jan 10;151(1):30-42
Authors: Choi MH, Xu J, Gutierrez M, Yoo T, Cho YH, Yoon SC
Polyhydroxyalkanoic acids (PHAs) and rhamnolipids considered as biotechnologically important...
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04-28-2011 03:12 PM
[CNS Yahoo group] Re: CNS Solve 1.3, "Bad CPU Type in Executable", OSX 10.6.6, Intel
Re: CNS Solve 1.3, "Bad CPU Type in Executable", OSX 10.6.6, Intel
Thanks Ben and others, here is the update so far, I installed gfortran (and gcc) from hpc.sourceforge.net, verified that they are installed by typing gcc and
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02-09-2011 08:23 PM
[CNS Yahoo group] Re: CNS Solve 1.3, "Bad CPU Type in Executable", OSX 10.6.6, Intel
Re: CNS Solve 1.3, "Bad CPU Type in Executable", OSX 10.6.6, Intel
... That would explain it, but then this in CNS installation instructions must be incorrect: "A binary installation is available for Intel Macintosh OS X,
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02-09-2011 08:23 PM
[CNS Yahoo group] Re: CNS Solve 1.3, "Bad CPU Type in Executable", OSX 10.6.6, Intel
Re: CNS Solve 1.3, "Bad CPU Type in Executable", OSX 10.6.6, Intel
(I added the list cc: back in for the archives.) Hi Nate, ... So that proves what you already know: you have a Core Duo machine, and those CPUs are 32-bit
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02-09-2011 08:23 PM
[CNS Yahoo group] Re: CNS Solve 1.3, "Bad CPU Type in Executable", OSX 10.6.6, Intel
Re: CNS Solve 1.3, "Bad CPU Type in Executable", OSX 10.6.6, Intel
Hi Nate, ... That only produces an error when running as root. The default user privilege on OS X only allows setting the max stacksize to the kernel max
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02-09-2011 08:23 PM
[NMR paper] Crystal structure and solution NMR dynamics of a D (type II) peroxiredoxin glutaredox
Crystal structure and solution NMR dynamics of a D (type II) peroxiredoxin glutaredoxin and thioredoxin dependent: a new insight into the peroxiredoxin oligomerism.
Related Articles Crystal structure and solution NMR dynamics of a D (type II) peroxiredoxin glutaredoxin and thioredoxin dependent: a new insight into the peroxiredoxin oligomerism.
Biochemistry. 2005 Feb 15;44(6):1755-67
Authors: Echalier A, Trivelli X, Corbier C, Rouhier N, Walker O, Tsan P, Jacquot JP, Aubry A, Krimm I, Lancelin JM
Peroxiredoxins (Prxs) constitute a family of...
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11-24-2010 11:14 PM
[NMR paper] NMR solution structure, backbone mobility, and homology modeling of c-type cytochrome
NMR solution structure, backbone mobility, and homology modeling of c-type cytochromes from gram-positive bacteria.
Related Articles NMR solution structure, backbone mobility, and homology modeling of c-type cytochromes from gram-positive bacteria.
Chembiochem. 2002 Apr 2;3(4):299-310
Authors: Banci L, Bertini I, Ciurli S, Dikiy A, Dittmer J, Rosato A, Sciara G, Thompsett AR
The solution structure of oxidized cytochrome c(553) (71 amino acid residues) from the Gram-positive bacterium Bacillus pasteurii is here reported and compared with the...
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11-24-2010 08:49 PM
[NMR paper] Proline pipe helix: structure of the tus proline repeat determined by 1H NMR.
Proline pipe helix: structure of the tus proline repeat determined by 1H NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Proline pipe helix: structure of the tus proline repeat determined by 1H NMR.
Biochemistry. 1996 Jan 23;35(3):698-703
Authors: Butcher DJ, Nedved ML, Neiss TG, Moe GR
The structure of a 22 amino acid peptide, TPPI , that is similar to the proline repeat segment of the replication arrest protein, Tus, has been determined by 1H NMR in 50% trifluroethanol. The...