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DR. DENIS P RALEIGH MD
MD
Thoracic Surgery (Cardiothoracic Vascular Surgery) Physician
NPI: 1427069855IndividualAccepts Medicare
Specialties, Licenses & Credentials
Thoracic Surgery (Cardiothoracic Vascular Surgery) PhysicianPrimary
Thoracic Surgery (Cardiothoracic Vascular Surgery)
Code: 208G00000X
MC-0944(ID)
Education
OTHER
Class of 1983
Research & Publications (20)
The unfolded state of the C-terminal domain of the ribosomal protein L9 contains both native and non-native structure.
PMID 19301913·Biochemistry·2009
8-other
A role for helical intermediates in amyloid formation by natively unfolded polypeptides?
PMID 19208933·Phys Biol·2009
8-other
Two-dimensional infrared spectroscopy provides evidence of an intermediate in the membrane-catalyzed assembly of diabetic amyloid.
PMID 19182939·J Phys Chem B·2009
7-preclinical
Experimental characterization of the denatured state ensemble of proteins.
PMID 19157090·Methods Mol Biol·2009
8-other
Interpretation of p-cyanophenylalanine fluorescence in proteins in terms of solvent exposure and contribution of side-chain quenchers: a combined fluorescence, IR and molecular dynamics study.
PMID 19658436·Biochemistry·2009
8-other
Partially folded equilibrium intermediate of the villin headpiece HP67 defined by 13C relaxation dispersion.
PMID 19644656·J Biomol NMR·2009
7-preclinical
Native like structure in the unfolded state of the villin headpiece helical subdomain, an ultrafast folding protein.
PMID 19598233·Protein Sci·2009
7-preclinical
A critical assessment of the role of helical intermediates in amyloid formation by natively unfolded proteins and polypeptides.
PMID 19596696·Protein Eng Des Sel·2009
6-review
Analysis of core packing in a cooperatively folded miniature protein: the ultrafast folding villin headpiece helical subdomain.
PMID 19354264·Biochemistry·2009
8-other
Two-dimensional IR spectroscopy and isotope labeling defines the pathway of amyloid formation with residue-specific resolution.
PMID 19346479·Proc Natl Acad Sci U S A·2009
8-other
Electrostatic interactions in the denatured state ensemble: their effect upon protein folding and protein stability.
PMID 17900519·Arch Biochem Biophys·2008
8-other
The fluorescent amino acid p-cyanophenylalanine provides an intrinsic probe of amyloid formation.
PMID 18478525·Chembiochem·2008
8-other
Characterizing septum inhibition in Mycobacterium tuberculosis for novel drug discovery.
PMID 18479968·Tuberculosis (Edinb)·2008
8-other
The low-pH unfolded state of the C-terminal domain of the ribosomal protein L9 contains significant secondary structure in the absence of denaturant but is no more compact than the low-pH urea unfolded state.
PMID 18707127·Biochemistry·2008
7-preclinical
Temperature-dependent Hammond behavior in a protein-folding reaction: analysis of transition-state movement and ground-state effects.
PMID 18384809·J Mol Biol·2008
8-other
Rifampicin does not prevent amyloid fibril formation by human islet amyloid polypeptide but does inhibit fibril thioflavin-T interactions: implications for mechanistic studies of beta-cell death.
PMID 18457428·Biochemistry·2008
8-other
Residue specific resolution of protein folding dynamics using isotope-edited infrared temperature jump spectroscopy.
PMID 17305369·Biochemistry·2007
8-other
Mutational analysis of the folding transition state of the C-terminal domain of ribosomal protein L9: a protein with an unusual beta-sheet topology.
PMID 17240985·Biochemistry·2007
8-other
Rational design, structural and thermodynamic characterization of a hyperstable variant of the villin headpiece helical subdomain.
PMID 17536785·Biochemistry·2007
8-other
Data courtesy of the U.S. National Library of Medicine (NLM). Ltrl is not affiliated with or endorsed by NLM.
Contact & Hours
- Address
- 3200 CHANNING WAY STE 205
IDAHO FALLS, ID 83404 - Phone
- (208) 535-4580
Quick Facts
- NPI
- 1427069855
- Entity Type
- Individual
- Gender
- Male
- Medicare
- Accepted
- Specialties
- 1
- Locations
- 1
- Years in Practice
- 43
- Publications
- 20
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