نتایج جستجو برای: conformational changes

تعداد نتایج: 897581  

2011
Jungkweon Choi Tetsuro Majima

In contrast to B-DNA that has a right-handed double helical structure with Watson–Crick base pairing under the ordinary physiological conditions, repetitive DNA sequences under certain conditions have the potential to fold into non-B DNA structures such as hairpin, triplex, cruciform, left-handed Z-form, tetraplex, A-motif, etc. Since the non-B DNA-forming sequences induce the genetic instabili...

Journal: :Journal of molecular biology 1999
S Subramaniam M Lindahl P Bullough A R Faruqi J Tittor D Oesterhelt L Brown J Lanyi R Henderson

We report a comprehensive electron crystallographic analysis of conformational changes in the photocycle of wild-type bacteriorhodopsin and in a variety of mutant proteins with kinetic defects in the photocycle. Specific intermediates that accumulate in the late stages of the photocycle of wild-type bacteriorhodopsin, the single mutants D38R, D96N, D96G, T46V, L93A and F219L, and the triple mut...

Journal: :Frontiers in bioscience 2014
Andrea Cristiani Fabio Maset Luca De Toni Diego Guidolin Davide Sabbadin Giacomo Strapazzon Stefano Moro Vincenzo De Filippis Carlo Foresta

Osteocalcin (OCN) is a small noncollagenous protein mainly produced by osteoblasts and is highly represented in bones of most vertebrates. Human OCN contains up to three gamma-carboxyglutamic acid (Gla-OCN) residues at positions 17, 21 and 24 which are thought to increase calcium binding strength, improving mechanical properties of the bone matrix. Recent studies revealed that OCN exerts also i...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 2013
Marie-Laure Rives Jonathan A Javitch

G protein-coupled receptors (GPCRs) are the largest and most diverse group of membrane receptors in eukaryotes and are targets of more than 25% of the medications currently on the market. Metabotropic glutamate receptors (mGluRs), family C GPCRs, modulate synaptic transmission and neuronal excitability throughout the central nervous system and thus are promising targets for the treatment of var...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 1978
V C Gordon C M Knobler D E Olins V N Schumaker

Hydrodynamic studies on monomer chromatin subunits (v1) as a function of ionic strength (0.7 mM to 100 mM KCl) indicate two salt-dependent conformational transitions. An abrupt transition occurs at about 7.5 mM ionic strength. Decreasing the ionic strength from 10 to 5 mM results in a decrease in s20,w of the v1 from 11.1 to 9.9 S. The diffusion coefficient D20,w decreases from 3.3 to 2.7 X 10(...

Journal: :Current opinion in structural biology 2004
Chern-Sing Goh Duncan Milburn Mark Gerstein

Motions related to protein-protein binding events can be surveyed from the perspective of the Database of Macromolecular Movements. There are a number of alternative conceptual models that describe these events, particularly induced fit and pre-existing equilibrium. There is evidence for both alternatives from recent studies of conformational change. However, there is increasing support for the...

2009
Tiago F. Outeiro Jochen Klucken Kathryn Bercury Julie Tetzlaff Preeti Putcha Luis M. A. Oliveira Alexandre Quintas Pamela J. McLean Bradley T. Hyman

BACKGROUND Oligomerization and aggregation of alpha-synuclein molecules play a major role in neuronal dysfunction and loss in Parkinson's disease [1]. However, alpha-synuclein oligomerization and aggregation have mostly been detected indirectly in cells using detergent extraction methods [2], [3], [4]. A number of in vitro studies showed that dopamine can modulate the aggregation of alpha-synuc...

Journal: :The Journal of biological chemistry 1968
G Markus E A Barnard B A Castellani D Saunders

The rate of formation of ribonuclease-S from ribonuclease A by the action of subtilisin was measured at pH 5.5 in the presence and absence of the strongly bound ribonuclease inhibitor, 2’-cytidylate. Presence of the inhibitor in the active center significantly reduced the rate of formation of ribonuclease-S. Since bond 20-21 (and, to a lesser extent, 21-22), the cleavage of which is responsible...

2008
Ronald Blaak Swen Lehmann Christos N. Likos

We study the effect of chargeable monomers on the conformation of dendrimers of low generation by computer simulations, employing bare Coulomb interactions. The presence of the latter leads to an increase in size of the dendrimer due to a combined effect of electrostatic repulsion and the presence of counterions within the dendrimer and also enhances a shell-like structure for the monomers of d...

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