Biomedical subjects

C E Strauss

Publications and source records attributed to C E Strauss.

4 recordsLinked to original sources

PubMed2001

Improving the performance of Rosetta using multiple sequence alignment information and global measures of hydrophobic core formation.

This study explores the use of multiple sequence alignment (MSA) information and global measures of hydrophobic core formation for improving the Rosetta ab initio protein structure prediction method. The most effective use of the MSA information is achieved by carrying out independent folding simulations for a subset of the homologous sequences in the MSA and then identifying the free energy minima common to all folded sequences via simultaneous clustering of the independent folding runs. Global measures of hydrophobic core formation, using ellipsoidal rather than spherical representations of the hydrophobic core, are found to be useful in removing non-native conformations before cluster analysis. Through this combination of MSA information and global measures of protein core formation, we significantly increase the performance of Rosetta on a challenging test set. Proteins 2001;43:1-11.

Algorithms↗

PubMed2001

Rosetta in CASP4: progress in ab initio protein structure prediction.

Rosetta ab initio protein structure predictions in CASP4 were considerably more consistent and more accurate than previous ab initio structure predictions. Large segments were correctly predicted (>50 residues superimposed within an RMSD of 6.5 A) for 16 of the 21 domains under 300 residues for which models were submitted. Models with the global fold largely correct were produced for several targets with new folds, and for several difficult fold recognition targets, the Rosetta models were more accurate than those produced with traditional fold recognition models. These promising results suggest that Rosetta may soon be able to contribute to the interpretation of genome sequence information.

Protein Conformation↗

PubMed2000

De novo protein structure determination using sparse NMR data.

We describe a method for generating moderate to high-resolution protein structures using limited NMR data combined with the ab initio protein structure prediction method Rosetta. Peptide fragments are selected from proteins of known structure based on sequence similarity and consistency with chemical shift and NOE data. Models are built from these fragments by minimizing an energy function that favors hydrophobic burial, strand pairing, and satisfaction of NOE constraints. Models generated using this procedure with approximately 1 NOE constraint per residue are in some cases closer to the corresponding X-ray structures than the published NMR solution structures. The method requires only the sparse constraints available during initial stages of NMR structure determination, and thus holds promise for increasing the speed with which protein solution structures can be determined.

Humans↗

PubMed1994

Lessons from medical treatment of Army Reserve units during annual training.

During annual training, a reserve hospital unit staffed a clinic, providing sick-call for its own members and secondary care for about 3,000 National Guard soldiers. Reservists reporting for sick call were treated predominantly for respiratory infection, while the Guard members complained most frequently of field-related injuries. Quality assurance (QA) was done by the authors to evaluate handling of sick call over the 2 weeks, and few problems emerged upon review of the clinic records. Suggestions for future years include establishing standard terminology for recording chief complaint and discharge disposition, and the use of treatment guidelines for training and QA purposes.

Guidelines as Topic↗