Abstract

ydrogen-bonding interactions are crucial to the function of many biological molecules. The vibrational modes associated with hydrogen bonds fall in the far-infrared region (150-250 cm-1). Actin is the primary component of muscle fibers. The single polypeptide unit is known as G-actin. When G-actin polymerizes to form actin filaments (i.e. muscle fibers), it is called F-actin. F-actin filaments are formed as two G actin monomers are twisted into a helix and it is thought that they are held together by a network of hydrogen-bonding interactions. Thus, a comparison of the far infrared spectra of G-Hversus F-actin provides a method for studying hydrogen-bonding interactions in proteins. We have grown films of G- and F-actin on polyethylene disks and determined their far infrared spectra. We observe 3 modes (532, 544, and 590 cm-1) in both G- and F-actin. In addition, we observe intense features in the F-actin spectrum at 181 and 254 cm-1, which are absent in the monomeric G-actin, and may be assignable to hydrogen bonding interactions in the F-actin. We plan to continue our studies on G- and F-actin by growing films under different conditions, such as in the presence of D2O and varying salt concentrations. D2O is expected to shift the frequency of hydrogen-bonding interactions and various salt conditions provide different levels of polymerization of G-actin into F-actin. In addition, the polarized nature of the infrared light will make it possible to study the orientation of the actin filaments.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
5P41RR001633-17
Application #
6205747
Study Section
Project Start
1999-09-01
Project End
2000-08-31
Budget Start
1998-10-01
Budget End
1999-09-30
Support Year
17
Fiscal Year
1999
Total Cost
Indirect Cost

  Institution

Name
Albert Einstein College of Medicine
Department
Type
DUNS #
009095365
City
Bronx
State
NY
Country
United States
Zip Code
10461

  Publications

Vongsvivut, Jitraporn; Fernandez, Jason; Ekgasit, Sanong et al. (2004) Characterization of supported cylinder-planar germanium waveguide sensors with synchrotron infrared radiation. Appl Spectrosc 58:143-51
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Huang, Raymond Y; Miller, Lisa M; Carlson, Cathy S et al. (2003) In situ chemistry of osteoporosis revealed by synchrotron infrared microspectroscopy. Bone 33:514-21
Rashidzadeh, Hassan; Khrapunov, Sergei; Chance, Mark R et al. (2003) Solution structure and interdomain interactions of the Saccharomyces cerevisiae ""TATA binding protein"" (TBP) probed by radiolytic protein footprinting. Biochemistry 42:3655-65
Uchida, Takeshi; Takamoto, Keiji; He, Qin et al. (2003) Multiple monovalent ion-dependent pathways for the folding of the L-21 Tetrahymena thermophila ribozyme. J Mol Biol 328:463-78
Taylor, Colleen M; Watton, Stephen P; Bryngelson, Peter A et al. (2003) Inner-sphere complexation of cobalt(II) 2,9-dimethyl-1,10-phenanthroline ([Co(neo)]2+) with commercial and sol-gel derived silica gel surfaces. Inorg Chem 42:312-20
Dewan, John C; Feeling-Taylor, Angela; Puius, Yoram A et al. (2002) Structure of mutant human carbonmonoxyhemoglobin C (betaE6K) at 2.0 A resolution. Acta Crystallogr D Biol Crystallogr 58:2038-42
Kiselar, J G; Maleknia, S D; Sullivan, M et al. (2002) Hydroxyl radical probe of protein surfaces using synchrotron X-ray radiolysis and mass spectrometry. Int J Radiat Biol 78:101-14
Swisher, Jennifer F; Su, Linhui J; Brenowitz, Michael et al. (2002) Productive folding to the native state by a group II intron ribozyme. J Mol Biol 315:297-310
Dhavan, Gauri M; Crothers, Donald M; Chance, Mark R et al. (2002) Concerted binding and bending of DNA by Escherichia coli integration host factor. J Mol Biol 315:1027-37

Showing the most recent 10 out of 68 publications