TITLE

Probing nanosecond protein motions of calmodulin by single-molecule fluorescence anisotropy

AUTHOR(S)
Xin Tan; Dehong Hu; Squier, Thomas C.; Lu, H. Peter
PUB. DATE
September 2004
SOURCE
Applied Physics Letters;9/20/2004, Vol. 85 Issue 12, p2420
SOURCE TYPE
Academic Journal
DOC. TYPE
Article
ABSTRACT
We report a single-molecule fluorescence anisotropy study of calmodulin, a regulatory protein for calcium-dependent cell signaling. Calmodulin in this study contains a site-specifically inserted tetra-cysteine motif that reacted with FlAsH, a biarsenic fluorescein derivative that can be rotationally locked to the host protein. A photon time-stamping technique was employed that combined the capability for both subnanosecond time resolution of time-correlated single photon counting and single-molecule time trajectory recording. The study provided direct characterization of the nanosecond motions of calmodulin tethered to a biologically compatible surface under physiological buffer solution. The unique technical approaches are applicable to single-molecule study of protein conformational dynamics and protein-protein interactions at a wide range of time scales and without the signal convolution of probe-dye molecular motions.
ACCESSION #
14546645

 

Related Articles

  • Elucidating the mechanisms of cooperative calcium-calmodulin interactions: a structural systems biology approach. Valeyev, Najl V.; Bates, Declan G.; Heslop-Harrison, Pat; Postlethwaite, Ian; Kotov, Nikolay V. // BMC Systems Biology;2008, Vol. 2, Special section p1 

    Background: Calmodulin is an important multifunctional molecule that regulates the activities of a large number of proteins in the cell. Calcium binding induces conformational transitions in calmodulin that make it specifically active to particular target proteins. The precise mechanisms...

  • Calmodulin Adopts an Extended Conformation when Interacting with L-Selectin in Membranes Deng, Wei; Putkey, John A.; Li, Renhao // PLoS ONE;May2013, Vol. 8 Issue 5, p1 

    Calmodulin, an intracellular calcium-binding protein, is thought to regulate ectodomain shedding of many membrane proteins, but the underlying molecular mechanism has remained unclear. Basing on a solution structure of calcium-loaded calmodulin in complex with a L-selectin fragment that contains...

  • Calmodulin.  // Encyclopedic Reference of Molecular Pharmacology;2004, p213 

    The article presents an encyclopedia entry for calmodulin, which is a protein that binds calcium.

  • Obtaining Site-Specific Calcium-Binding Affinities Of Calmodulin. Jenny J. Yang; Amy Gawthrop; Yiming Ye // Protein & Peptide Letters;Aug2003, Vol. 10 Issue 4, p331 

    Calmodulin (CaM) is an EF-hand Ca(II)-binding protein involved in the regulation of many important biological processes. To date, there is a wealth of information available concerning studies to obtain site-specific calcium binding affinities of CaM, and further to estimate the cooperativity of...

  • Differential modulation of Cav2.1 channels by calmodulin and Ca2+-binding protein 1. Lee, Amy; Westenbroek, Ruth E.; Haeseleer, Françoise; Palczewski, Krzysztof; Scheuer, Todd; Catterall, William A. // Nature Neuroscience;Mar2002, Vol. 5 Issue 3, p210 

    Ca[sub v]2.1 channels, which mediate P/Q-type Ca[sup 2+] currents, undergo Ca[sup 2+]/calmodulin (CaM)dependent inactivation and facilitation that can significantly alter synaptic efficacy. Here we report that the neuronal Ca[sup 2+]-binding protein 1 (CaBP1) modulates Ca[sub v]2.1 channels in a...

  • Calmodulin.  // British Medical Journal;12/6/1980, Vol. 281 Issue 6254, p1510 

    Examines the multiple function of calmodulin in the body. Uniqueness of calmodulin among calcium-binding proteins; Recall on the major scientific achievements of Heilbrunn and Wiercinski on the study of calmodulin; Implications for biological potency of calmodulin.

  • FhCaBP4: a Fasciola hepatica calcium-binding protein with EF-hand and dynein light chain domains. Orr, Rebecca; Kinkead, Ruth; Newman, Richard; Anderson, Lindsay; Hoey, Elizabeth; Trudgett, Alan; Timson, David // Parasitology Research;Oct2012, Vol. 111 Issue 4, p1707 

    In trematodes, there is a family of proteins which combine EF-hand-containing domains with dynein light chain (DLC)-like domains. A member of this family from the liver fluke, Fasciola hepatica-FhCaBP4-has been identified and characterised biochemically. FhCaBP4 has an N-terminal domain...

  • Key genes associated with osteoporosis revealed by genome wide gene expression analysis. Chen, Jie; Wang, Lei; Shen, Yuhui; Yu, Jian; Ye, Tingjun; Zhuang, Chengyu; Zhang, Weibin // Molecular Biology Reports;Sep2014, Vol. 41 Issue 9, p5971 

    Gene expression profiles of circulating monocytes were analyzed to identify key genes associated with osteoporosis. Raw microarray data were downloaded from gene expression omnibus under accession number GSE7158, including 8 microarray dataset for patients with high peak bone mass (PBM) and 8...

  • Membrane Interactions of S100A12 (Calgranulin C). Garcia, Assuero F.; Lopes, José L. S.; Costa-Filho, Antonio J.; Wallace, Bonnie A.; Araujo, Ana P. U. // PLoS ONE;Dec2013, Vol. 8 Issue 12, p1 

    S100A12 (Calgranulin C) is a small acidic calcium-binding peripheral membrane protein with two EF-hand structural motifs. It is expressed in macrophages and lymphocytes and highly up-regulated in several human inflammatory diseases. In pigs, S100A12 is abundant in the cytosol of granulocytes,...

Share

Read the Article

Courtesy of VIRGINIA BEACH PUBLIC LIBRARY AND SYSTEM

Sorry, but this item is not currently available from your library.

Try another library?
Sign out of this library

Other Topics