S. Decatur

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Insights from a Convocation: Integrating Discovery-Based Research into the Undergraduate Curriculum

Wendy C. Newstetter, Laura Guertin, Jay B. Labov, 2016, CBE life sciences education.

Anatomy and dynamics of a ligand-binding pathway in myoglobin: the roles of residues 45, 60, 64, and 68.

S. Boxer, D. Lambright, S G Boxer, 1994, Biochemistry.

Different modes of binding of mono-, di-, and trihalogenated phenols to the hemoglobin dehaloperoxidase from Amphitrite ornata.

Michael F. Davis, Franck A. P. Vendeix, S. Franzen, 2009, Biochemistry.

Analysis of local conformation within helical peptides via isotopeedited vibrational spectroscopy

P. Bouř, T. Keiderling, R. A. Silva, 2002 .

Amyloid fiber formation in human γD-Crystallin induced by UV-B photodamage.

M. Zanni, S. Decatur, S. Moran, 2013, Biochemistry.

PEPTIDES USEFUL IN THE TREATMENT AND/OR CARE OF SKIN, MUCOUS MEMBRANES, SCALP AND/OR HAIR AND THEIR USE IN COSMETIC OR PHARMACEUTICAL COMPOSITIONS-European Patent Office-EP 2331560 B1

S. Decatur, 2019 .

Elucidation of residue-level structure and dynamics of polypeptides via isotope-edited infrared spectroscopy.

S. Decatur, 2006, Accounts of chemical research.

Trans effects in nitric oxide binding to myoglobin cavity mutant H93G.

S. Boxer, S. Franzen, W. Woodruff, 1996, Biochemistry.

A test of the role of electrostatic interactions in determining the CO stretch frequency in carbonmonoxymyoglobin.

S. Boxer, S. Decatur, 1995, Biochemical and biophysical research communications.

Vibrational Dynamics of Carbon Monoxide at the Active Sites of Mutant Heme Proteins

S. Boxer, M. Fayer, D. Dlott, 1996 .

Site-specific conformational determination in thermal unfolding studies of helical peptides using vibrational circular dichroism with isotopic substitution.

P. Bouř, T. Keiderling, J. Kubelka, 2000, Proceedings of the National Academy of Sciences of the United States of America.

Self-aggregation of a polyalanine octamer promoted by its C-terminal tyrosine and probed by a strongly enhanced vibrational circular dichroism signal.

T. Measey, Liming Zhao, S. Decatur, 2009, Journal of the American Chemical Society.

Two-dimensional IR spectroscopy and segmental 13C labeling reveals the domain structure of human γD-crystallin amyloid fibrils

L. Buchanan, M. Zanni, S. Decatur, 2012, Proceedings of the National Academy of Sciences.

Intersheet rearrangement of polypeptides during nucleation of β-sheet aggregates

Sarah A. Petty, Sean M. Decatur, S. Decatur, 2005 .

Experimental Evidence for the Reorganization of β-Strands within Aggregates of the Aβ(16−22) Peptide

S. Decatur, S. Petty, 2005 .

Nature of vibrational coupling in helical peptides: an isotopic labeling study.

T. Keiderling, J. Kubelka, R. A. Silva, 2004, Journal of the American Chemical Society.

The organization and assembly of a beta-sheet formed by a prion peptide in solution: an isotope-edited FTIR study.

R. A. Silva, S. Decatur, W. Barber-Armstrong, 2003, Journal of the American Chemical Society.

Elucidation of Residue-Level Structure and Dynamics of Polypeptides via Isotope-Edited Infrared Spectroscopy

S. Decatur, 2006 .

ChemInform Abstract: Chirality in Peptide Vibrations: ab initio Computational Studies of Length, Solvation, Hydrogen Bond, Dipole Coupling, and Isotope Effects on Vibrational CD.

P. Bouř, T. Keiderling, J. Kubelka, 2002 .

Two-dimensional infrared measurements of the coupling between amide modes of an α-helix

R. Hochstrasser, Chong Fang, Amos B. Smith, 2003 .

Differential effects of phe19 and phe20 on fibril formation by amyloidogenic peptide Aβ16–22 (Ac‐KLVFFAE‐NH2)

D. Kirschner, Dong Zhang, S. Decatur, 2010, Proteins.

Probing the effect of side chains on the conformation and stability of helical peptides via isotope-edited infrared spectroscopy.

R. A. Silva, S. Decatur, Julie Nguyen, 2002, Biochemistry.

IR spectroscopy of isotope-labeled helical peptides: probing the effect of N-acetylation on helix stability.

S. Decatur, 2000, Biopolymers.

Isotope-Edited Infrared Spectroscopy of Helical Peptides

J. Antonic, S. Decatur, 1999 .

FUNCTIONAL CAVITIES IN PROTEINS : A GENERAL METHOD FOR PROXIMAL LIGAND SUBSTITUTION IN MYOGLOBIN

Doug Barrick, S. Boxer, D. Barrick, 1994 .

Spectroscopic evidence for backbone desolvation of helical peptides by 2,2,2-trifluoroethanol: an isotope-edited FTIR study.

S. Decatur, W. Barber-Armstrong, M. Sridharan, 2005, Biochemistry.

Fiber diffraction as a screen for amyloid inhibitors.

D. Kirschner, S. Decatur, H. Inouye, 2008, Current Alzheimer research.

Formation of amyloid fibrils in vitro by human γD-crystallin and its isolated domains

J. King, D. Kirschner, S. Thol, 2008, Molecular vision.

Modulation of protein function by exogenous ligands in protein cavities: CO binding to a myoglobin cavity mutant containing unnatural proximal ligands.

S. Boxer, S G Boxer, G D DePillis, 1996, Biochemistry.

1H NMR characterization of myoglobins where exogenous ligands replace the proximal histidine.

S. Boxer, S. Decatur, 1995, Biochemistry.

Experimental evidence for the reorganization of beta-strands within aggregates of the Abeta(16-22) peptide.

S. Decatur, S. Petty, 2005, Journal of the American Chemical Society.

Two-dimensional infrared spectroscopy of isotopomers of an alanine rich α-helix

R. Hochstrasser, Chong Fang, Jianping Wang, 2004 .

Structural and sequence analysis of the human γD-crystallin amyloid fibril core using 2D IR spectroscopy, segmental 13C labeling, and mass spectrometry.

M. Zanni, S. Decatur, S. Moran, 2012, Journal of the American Chemical Society.

Amide I Frequency as a Probe of Tertiary Structure: FTIR Studies of Helix Bundle Peptides

S. Decatur, K. Monteiro, W. Barber-Armstrong, 2001 .

Vibrational circular dichroism with isotopic substitution. Application to alanine rich peptides

P. Bouř, T. Keiderling, R. A. Silva, 1999 .

The alpha-helix folds more rapidly at the C-terminus than at the N-terminus.

M. Volk, S. Decatur, S. Petty, 2005, Journal of the American Chemical Society.

Differential effects of phe19 and phe20 on fibril formation by amyloidogenic peptide Aβ16–22 (Ac‐KLVFFAE‐NH2)

Dong Zhang, S. Decatur, H. Inouye, 2010, Proteins.

Correlations among morphology, beta-sheet stability, and molecular structure in prion peptide aggregates.

T. Adalsteinsson, S. Decatur, Thorsteinn Adalsteinsson, 2005, Biochemistry.

Intersheet rearrangement of polypeptides during nucleation of {beta}-sheet aggregates.

S. Decatur, S. Petty, 2005, Proceedings of the National Academy of Sciences of the United States of America.