Albert Beth
Last active: 2/23/2015

Profile

Intrinsic membrane proteins serve a number of essential functions in all cells. These functions include substrate transport, signalling, and membrane stabilization to cite a few. Despite their abundance (approximately 1/3 of the human genome), their essential functions in normal physiology, and their involvement in many diseases, relatively little is known about the structures of most membrane proteins. This is due in large part to the fact that the membrane proteins are not generally amenable to structural characterization using classical techniques such as X-ray crystallography and NMR. Our laboratory is involved in the development and application of new spectroscopic approaches to determine the structures of intrinsic membrane proteins including how structural rearrangements modulate their biological functions.

Specifically, we are employing spectroscopic techniques including electron paramagnetic resonance, nuclear magnetic resonance, and fluorescence to characterize the structure, dynamics and interactions of the anion exchange protein in human erythrocytes, the receptor for epidermal growth factor (EGF) in A-431 cells and the 5-HT3 receptor in neurons.

Specific questions currently being addressed include: What are the structures of the transmembrane and cytoplasmic domains of the anion exchange protein? What is the nature and extent of interactions between the cytoplasmic domain of the anion exchange protein and the extensive membrane skeleton and how are these interactions altered in erythrocytes exhibiting abnormal fragility from patients with hemolytic anemias? What are the oligomeric structures of the anion exchange protein and the EGF receptor in their native membranes? What molecular rearrangements occur in the EGF receptor upon EGF binding and how are these changes related temporally to activation of its tyrosine kinase activity? How are the subunits of the 5-HT3 receptor arranged and how does this structure lead to the formation of a ligand-gated ion channel? How do compounds that modeulate the function of the 5-HT3 receptor such as ethanol and anesthetics alter its structure and interactions?

Publications

The following timeline graph is generated from all co-authored publications.

Featured publications are shown below:

  1. Automated structure refinement for a protein heterodimer complex using limited EPR spectroscopic data and a rigid-body docking algorithm: a three-dimensional model for an ankyrin-CDB3 complex. Edwards SJ, Moth CW, Kim S, Brandon S, Zhou Z, Cobb CE, Hustedt EJ, Beth AH, Smith JA, Lybrand TP (2014) J Phys Chem B 118(18): 4717-26
    › Primary publication · 24758720 (PubMed) · PMC4018176 (PubMed Central)
  2. Structural arrangement of the intracellular Ca2+ binding domains of the cardiac Na+/Ca2+ exchanger (NCX1.1): effects of Ca2+ binding. Dixit M, Kim S, Matthews GF, Erreger K, Galli A, Cobb CE, Hustedt EJ, Beth AH (2013) J Biol Chem 288(6): 4194-207
    › Primary publication · 23233681 (PubMed) · PMC3567668 (PubMed Central)
  3. Rotational diffusion of membrane proteins: characterization of protein-protein interactions in membranes. Beth AH (2012) Biophys J 103(6): 1109
    › Primary publication · 22995482 (PubMed) · PMC3446685 (PubMed Central)
  4. The global analysis of DEER data. Brandon S, Beth AH, Hustedt EJ (2012) J Magn Reson : 93-104
    › Primary publication · 22578560 (PubMed) · PMC3608411 (PubMed Central)
  5. Determination of structural models of the complex between the cytoplasmic domain of erythrocyte band 3 and ankyrin-R repeats 13-24. Kim S, Brandon S, Zhou Z, Cobb CE, Edwards SJ, Moth CW, Parry CS, Smith JA, Lybrand TP, Hustedt EJ, Beth AH (2011) J Biol Chem 286(23): 20746-57
    › Primary publication · 21493712 (PubMed) · PMC3121456 (PubMed Central)
  6. Structure of the cytoplasmic domain of erythrocyte band 3 hereditary spherocytosis variant P327R: band 3 Tuscaloosa. Zhou Z, DeSensi SC, Stein RA, Brandon S, Song L, Cobb CE, Hustedt EJ, Beth AH (2007) Biochemistry 46(36): 10248-57
    › Primary publication · 17696498 (PubMed)
  7. Solution structure of the cytoplasmic domain of erythrocyte membrane band 3 determined by site-directed spin labeling. Zhou Z, DeSensi SC, Stein RA, Brandon S, Dixit M, McArdle EJ, Warren EM, Kroh HK, Song L, Cobb CE, Hustedt EJ, Beth AH (2005) Biochemistry 44(46): 15115-28
    › Primary publication · 16285715 (PubMed)
  8. Rotational dynamics of the epidermal growth factor receptor. Stein RA, Hustedt EJ, Staros JV, Beth AH (2002) Biochemistry 41(6): 1957-64
    › Primary publication · 11827542 (PubMed)
  9. Flexibility of the cytoplasmic domain of the anion exchange protein, band 3, in human erythrocytes. Blackman SM, Hustedt EJ, Cobb CE, Beth AH (2001) Biophys J 81(6): 3363-76
    › Primary publication · 11720999 (PubMed) · PMC1301793 (PubMed Central)
  10. The sensitivity of saturation transfer electron paramagnetic resonance spectra to restricted amplitude uniaxial rotational diffusion. Hustedt EJ, Beth AH (2001) Biophys J 81(6): 3156-65
    › Primary publication · 11720982 (PubMed) · PMC1301776 (PubMed Central)