Results 71 to 80 of about 10,126,895 (308)

Crystal structures of the human Dysferlin inner DysF domain [PDF]

, 2014
Background: Mutations in dysferlin, the first protein linked with the cell membrane repair mechanism, causes a group of muscular dystrophies called dysferlinopathies.
Cole, Ambrose R., Nicholas H Keep, Keep, Nicholas H., Altin Sula, Sula, Altin, Orengo, C., Ambrose R Cole, Corin Yeats, Yeats, C., Christine Orengo   +9 more
core   +1 more source

EFFECT OF L,α-ALANINE IMPURITY ON THE SPONTANEOUS EVOLUTION OF THE DOMAIN STRUCTURE OF TRIGLICINE SULPHATE NEAR THE CURIE POINT

Конденсированные среды и межфазные границы, 2018
Using the atomic force microscopy method in the piezoelectric response mode, the evolution of the nonequilibrium domain structure of pure triglycine sulfate (TGS) crystals and doped with an L, α-alanine (ATGS) impurity was studied near the phase ...
Olga M. Golitsyna, Sergey N. Drozhdin, Valeriya O. Lesnikova   +2 more
doaj   +1 more source

FRACTAL ANALYSIS OF THE MAZE-LIKE DOMAIN STRUCTURE OF FERRITE-GARNET FILMS IN THE PROCESS OF MAGNETIZATION

Физико-химические аспекты изучения кластеров, наноструктур и наноматериалов, 2021
In this work, using a set of experimental techniques and specialized software, magnetic bismuth-containing ferrite-garnet films grown on gadolinium-gallium garnet substrates are investigated.
A.D. Zigert, G.G. Dunaeva, N.Yu. Sdobnyakov   +2 more
doaj   +1 more source

Exploring protein domain structure [PDF]

Briefings in Bioinformatics, 2000
The protein databank contains coordinates of over 10,000 protein structures, which constitute more than 25,000 structural domains in total. The investigation of protein structural, functional and evolutionary relationships is fundamental to many important fields in bioinformatics research, and will be crucial in determining the function of the human ...
openaire   +2 more sources

Domain structure of riboflavin synthase [PDF]

European Journal of Biochemistry, 2001
Riboflavin synthase of Escherichia coli is a homotrimer of 23.4 kDa subunits catalyzing the formation of the carbocyclic ring of the vitamin, riboflavin, by dismutation of 6,7‐dimethyl‐8‐ribityllumazine. Intramolecular sequence similarity suggested that each subunit folds into two topologically similar domains.
S, Eberhardt, N, Zingler, K, Kemter, G, Richter, M, Cushman, A, Bacher   +5 more
openaire   +2 more sources

Organizing the interface—Plasma membrane architecture and receptor dynamics in virus‐cell interactions

FEBS Letters, EarlyView.
Plasma membranes contain dynamic nanoscale domains that organize lipids and receptors. Because viruses operate at similar scales, this architecture shapes early infection steps, including attachment, receptor engagement, and entry. Using influenza A virus and HIV‐1 as examples, we highlight how receptor nanoclusters, multivalent glycan interactions ...
Jan Schlegel, Christian Sieben
wiley   +1 more source

THERMAL-INDUCED DOMAIN PROCESSES IN TRIGLYCINE SULFATE CRYSTALS WITH CHROMIUM IMPURITIES

Физико-химические аспекты изучения кластеров, наноструктур и наноматериалов, 2021
The article presents the results of studies of thermally induced domain processes in chromium-containing crystals of triglycine sulfate (TGS). It is shown that a change in the temperature of TGS:Cr3+ crystals in the absence of external electric fields ...
N.N. Bolshakova, E.V. Vahterov, A.I. Ivanova, B.B. Ped`ko, E.M. Semenova   +4 more
doaj   +1 more source

Protein structural domain identification [PDF]

Protein Engineering, Design and Selection, 1999
A simple method for the definition of protein structural domains is described that requires only alpha-carbon coordinate data. The basic method, which encodes no specific aspects of protein structure, captures the essence of most domains but does not give high enough priority to the integrity of beta-sheet structure.
openaire   +2 more sources

Septin 9 PB domains coordinate centrosome positioning and microtubule acetylation to control epithelial polarity

FEBS Letters, EarlyView.
Septin 9 polybasic domains couple phosphoinositide‐rich membrane binding to centrosome positioning, Golgi organization, and microtubule acetylation to control epithelial polarity. Their loss disrupts this axis, causing centrosome mispositioning, Golgi fragmentation, reduced microtubule acetylation, and polarity inversion via upregulation of the ...
Ting ting Cai, Mohyeddine Omrane, Nassima Benzoubir, Didier Samuel, Ama Gassama‐Diagne   +4 more
wiley   +1 more source

Structural and functional analyses of PAS domain interactions of the clock proteins Drosophila PERIOD and mouse PERIOD2 [PDF]

, 2009
PERIOD proteins are central components of the Drosophila and mammalian circadian clocks. The crystal structure of a Drosophila PERIOD (dPER) fragment comprising two PER-ARNT-SIM (PAS) domains (PAS-A and PAS-B) and two additional C-terminal alpha-helices (
Strauss, Holger M, Wolf, Eva, Schulze, Sabrina, Sven Hennig, Arens, J., Hennig, Sven; id_orcid, Yildiz, O., Strauss, Holger M., Holger M Strauss, Julia Arens, Kramer, Achim, Arens, Julia, Sabrina Schulze, Schulze, S., Eva Wolf, Vanselow, Katja, Yildiz, Özkan, Katja Vanselow, Strauss, H., Hennig, S., Kramer, A., Vanselow, K., Wolf, E., Strauss, H. M., Achim Kramer, Ozkan Yildiz, Hennig, Sven   +26 more
core   +1 more source