Mr. Denis P Raleigh MD
Cardiothoracic Surgeon
2315 Green Valley Rd Suite 200 New Albany IN, 47150Rating
4/5
About
Dr. Denis Raleigh is a cardiothoracic surgeon practicing in New Albany, IN. Dr. Raleigh specializes in surgical procedues of vital organs in the chest such as the heart, lungs, esophagus and more. As a cardiothoracic surgeon, Dr. Raleigh typically treats conditions like heart disease and lung disease. This class of surgeon can also include cardiac surgeons, cardiovascular surgeons, congenital heart surgeons and general thoracic surgeons.
Board Certification
Thoracic SurgeryAmerican Board of Thoracic SurgeryABTS
Provider Details
Expert Publications
Data provided by the National Library of Medicine- Effects of sequential proline substitutions on amyloid formation by human amylin20-29.
- Conformational analysis of peptide fragments derived from the peripheral subunit-binding domain from the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus: evidence for nonrandom structure in the unfolded state.
- Conformational analysis of a set of peptides corresponding to the entire primary sequence of the N-terminal domain of the ribosomal protein L9: evidence for stable native-like secondary structure in the unfolded state.
- Nativelike structure and stability in a truncation mutant of a protein minidomain: the peripheral subunit-binding domain.
- pKa values and the pH dependent stability of the N-terminal domain of L9 as probes of electrostatic interactions in the denatured state. Differentiation between local and nonlocal interactions.
- Folding of the multidomain ribosomal protein L9: the two domains fold independently with remarkably different rates.
- Effects of varying the local propensity to form secondary structure on the stability and folding kinetics of a rapid folding mixed alpha/beta protein: characterization of a truncation mutant of the N-terminal domain of the ribosomal protein L9.
- Local interactions drive the formation of nonnative structure in the denatured state of human alpha-lactalbumin: a high resolution structural characterization of a peptide model in aqueous solution.
- Submillisecond folding of the peripheral subunit-binding domain.
- Defining the core structure of the alpha-lactalbumin molten globule state.
- Analysis of amylin cleavage products provides new insights into the amyloidogenic region of human amylin.
- Local interactions and the role of the 6-120 disulfide bond in alpha-lactalbumin: implications for formation of the molten globule state.
- Rational modification of protein stability by the mutation of charged surface residues.
- Solution structure of a peptide model of a region important for the folding of alpha-lactalbumin provides evidence for the formation of nonnative structure in the denatured state.
- pH jump studies of the folding of the multidomain ribosomal protein L9: the structural organization of the N-terminal domain does not affect the anomalously slow folding of the C-terminal domain.
Mr. Denis P Raleigh MD's Practice location
Practice At 2315 Green Valley Rd Suite 200
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BAPTIST HEALTH FLOYDl
1850 STATE ST NEW ALBANY IN 47150