Abstract

This proposal seeks continued funding for studies of application of vibrational optical activity techniques to biologically interesting molecules. We plan to develop consistent empirical descriptions of the relationship between structure and spectra for several biopolymeric systems. The main thrust will be development of understanding of oligopeptide conformations via VCD (vibrational circular dichroism). This data will be most relevant to protein structure and an extensive effort to correlate such data to globular protein VCD will be attempted. Other applications will include membrane proteins and oligopeptide drugs. Our development of techniques and polypeptide spectra-structure relationships is reviewed in the proposal. Similar efforts will be undertaken to develop systematic understanding of polynucleotide VCD for subsequent studies of detailed environmental effects on nucleic acid conformations. Application to biochemically relevant systems will require use of aqueous environments with a consequent loss of signal-to-noise ratio. To overcome this we will add FT-IR VCD capability to our laboratory which will additionally enable a more intensive effort to be devoted to these problems.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM030147-05
Application #
3277763
Study Section
Biophysics and Biophysical Chemistry A Study Section (BBCA)
Project Start
1982-02-01
Project End
1988-06-30
Budget Start
1986-07-01
Budget End
1987-06-30
Support Year
5
Fiscal Year
1986
Total Cost
Indirect Cost

  Institution

Name
University of Illinois at Chicago
Department
Type
Schools of Arts and Sciences
DUNS #
121911077
City
Chicago
State
IL
Country
United States
Zip Code
60612

  Publications

Keiderling, Timothy A; Xu, Q (2002) Unfolded peptides and proteins studied with infrared absorption and vibrational circular dichroism spectra. Adv Protein Chem 62:111-61
Silva, R A Gangani D; Yasui, Sritana C; Kubelka, Jan et al. (2002) Discriminating 3(10)- from alpha-helices: vibrational and electronic CD and IR absorption study of related Aib-containing oligopeptides. Biopolymers 65:229-43
Baello, B I; Pancoska, P; Keiderling, T A (2000) Enhanced prediction accuracy of protein secondary structure using hydrogen exchange Fourier transform infrared spectroscopy. Anal Biochem 280:46-57
Bour, P; Kubelka, J; Keiderling, T A (2000) Simulations of oligopeptide vibrational CD: effects of isotopic labeling. Biopolymers 53:380-95
Pancoska, P; Janota, V; Keiderling, T A (1999) Novel matrix descriptor for secondary structure segments in proteins: demonstration of predictability from circular dichroism spectra. Anal Biochem 267:72-83
Silva, R A; Sherman, S A; Keiderling, T A (1999) Beta-hairpin stabilization in a 28-residue peptide derived from the beta-subunit sequence of human chorionic gonadotropin hormone. Biopolymers 50:413-23
Keiderling, T A; Silva, R A; Yoder, G et al. (1999) Vibrational circular dichroism spectroscopy of selected oligopeptide conformations. Bioorg Med Chem 7:133-41
Lusitani, D; Menhart, N; Keiderling, T A et al. (1998) Ionic strength effect on the thermal unfolding of alpha-spectrin peptides. Biochemistry 37:16546-54
Wi, S; Pancoska, P; Keiderling, T A (1998) Predictions of protein secondary structures using factor analysis on Fourier transform infrared spectra: effect of Fourier self-deconvolution of the amide I and amide II bands. Biospectroscopy 4:93-106
Yoder, G; Pancoska, P; Keiderling, T A (1997) Characterization of alanine-rich peptides, Ac-(AAKAA)n-GY-NH2 (n = 1-4), using vibrational circular dichroism and Fourier transform infrared. Conformational determination and thermal unfolding. Biochemistry 36:15123-33

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