scholarly journals Biophysical studies support a predicted superhelical structure with armadillo repeats for Ric-8

2009 ◽  
Vol 18 (6) ◽  
pp. 1139-1145 ◽  
Author(s):  
Maximiliano Figueroa ◽  
María Victoria Hinrichs ◽  
Marta Bunster ◽  
Patricia Babbitt ◽  
José Martinez-Oyanedel ◽  
...  
Keyword(s):  
Biophysical Studies ◽  
Superhelical Structure ◽  
Armadillo Repeats

scholarly journals Insight into the HIV-1 Vif SOCS-box–ElonginBC interaction

Open Biology ◽  
2013 ◽  
Vol 3 (11) ◽  
pp. 130100 ◽  
Author(s):  
Zhisheng Lu ◽  
Julien R. C. Bergeron ◽  
R. Andrew Atkinson ◽  
Torsten Schaller ◽  
Dennis A. Veselkov ◽  
...  
Keyword(s):  
Solution Structure ◽  
Hydrophobic Interactions ◽  
Dynamic Information ◽  
Ubiquitin Ligase Complex ◽  
Biophysical Studies ◽  
Viral Infectivity Factor ◽  
Β Sheet ◽  
Socs Box ◽  
Insight Into ◽  
Hiv 1

The HIV-1 viral infectivity factor (Vif) neutralizes cell-encoded antiviral APOBEC3 proteins by recruiting a cellular ElonginB (EloB)/ElonginC (EloC)/Cullin5-containing ubiquitin ligase complex, resulting in APOBEC3 ubiquitination and proteolysis. The suppressors-of-cytokine-signalling-like domain (SOCS-box) of HIV-1 Vif is essential for E3 ligase engagement, and contains a BC box as well as an unusual proline-rich motif. Here, we report the NMR solution structure of the Vif SOCS–ElonginBC (EloBC) complex. In contrast to SOCS-boxes described in other proteins, the HIV-1 Vif SOCS-box contains only one α-helical domain followed by a β-sheet fold. The SOCS-box of Vif binds primarily to EloC by hydrophobic interactions. The functionally essential proline-rich motif mediates a direct but weak interaction with residues 101–104 of EloB, inducing a conformational change from an unstructured state to a structured state. The structure of the complex and biophysical studies provide detailed insight into the function of Vif's proline-rich motif and reveal novel dynamic information on the Vif–EloBC interaction.

scholarly journals BIOPHYSICAL STUDIES OF BLOOD PLASMA PROTEINS

1946 ◽  
Vol 165 (1) ◽  
pp. 21-35 ◽  
Author(s):  
H.F. Deutsch ◽  
R.A. Alberty ◽  
L.J. Gosting
Keyword(s):  
Blood Plasma ◽  
Plasma Proteins ◽  
Biophysical Studies ◽  
Blood Plasma Proteins

scholarly journals Biophysical studies of cholesterol effects on chromatin

2017 ◽  
Vol 58 (5) ◽  
pp. 934-940 ◽  
Author(s):  
Isabel T. G. Silva ◽  
Vinícius Fernandes ◽  
Caio Souza ◽  
Werner Treptow ◽  
Guilherme M. Santos
Keyword(s):  
Biophysical Studies

Biochemical and biophysical studies of the interaction of class I antiarrhythmic drugs with the cardiac sodium channel

1994 ◽  
Vol 33 (3) ◽  
pp. 277-294 ◽  
Author(s):  
Gerald W. Zamponi ◽  
Henry J. Duff ◽  
Robert J. French ◽  
Robert S. Sheldon
Keyword(s):  
Sodium Channel ◽  
Antiarrhythmic Drugs ◽  
Class I ◽  
Cardiac Sodium Channel ◽  
Biophysical Studies

Biophysical Studies of the Immunoglobulins

1971 ◽  
Vol 40 (4-5) ◽  
pp. 551-575 ◽  
Author(s):  
G.W. Litman ◽  
A. Rosenberg ◽  
D. Frommel ◽  
B. Pollara ◽  
J. Finstad ◽  
...  
Keyword(s):  
Biophysical Studies

scholarly journals PF16 encodes a protein with armadillo repeats and localizes to a single microtubule of the central apparatus in Chlamydomonas flagella.

1996 ◽  
Vol 132 (3) ◽  
pp. 359-370 ◽  
Author(s):  
E F Smith ◽  
P A Lefebvre
Keyword(s):  
Protein Interactions ◽  
Insertional Mutagenesis ◽  
Flagellar Motility ◽  
Wild Type ◽  
Protein Protein Interactions ◽  
Cellular Functions ◽  
Central Pair ◽  
Central Apparatus ◽  
Immunofluorescence Labeling ◽  
Armadillo Repeats

Several studies have indicated that the central pair of microtubules and their associated structures play a significant role in regulating flagellar motility. To begin a molecular analysis of these components we have generated central apparatus-defective mutants in Chlamydomonas reinhardtii using insertional mutagenesis. One paralyzed mutant recovered in our screen, D2, is an allele of a previously identified mutant, pf16. Mutant cells have paralyzed flagella, and the C1 microtubule of the central apparatus is missing in isolated axonemes. We have cloned the wild-type PF16 gene and confirmed its identity by rescuing pf16 mutants upon transformation. The rescued pf16 cells were wild-type in motility and in axonemal ultrastructure. A full-length cDNA clone for PF16 was obtained and sequenced. Database searches using the predicted 566 amino acid sequence of PF16 indicate that the protein contains eight contiguous armadillo repeats. A number of proteins with diverse cellular functions also contain armadillo repeats including pendulin, Rch1, importin, SRP-1, and armadillo. An antibody was raised against a fusion protein expressed from the cloned cDNA. Immunofluorescence labeling of wild-type flagella indicates that the PF16 protein is localized along the length of the flagella while immunogold labeling further localizes the PF16 protein to a single microtubule of the central pair. Based on the localization results and the presence of the armadillo repeats in this protein, we suggest that the PF16 gene product is involved in protein-protein interactions important for C1 central microtubule stability and flagellar motility.

scholarly journals Effect of superhelical structure on the secondary structure of DNA rings

Biopolymers ◽  
1967 ◽  
Vol 5 (8) ◽  
pp. 691-696 ◽  
Author(s):  
Daniel Glaubiger ◽  
John E. Hearst
Keyword(s):  
Secondary Structure ◽  
Superhelical Structure
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