MARC Record from Library of Congress

LEADER: 04336cam a22004577i 4500
001 2014930165
003 DLC
005 20140626092634.0
008 140106t20142014sz a b 001 0 eng d
010 $a 2014930165
020 $a9783319029696 (alk. paper)
020 $a331902969X (alk. paper)
020 $z9783319029702 (ebook)
020 $z3319029703 (ebook)
035 $a(OCoLC)ocn871193503
040 $aCDX$beng$cCDX$erda$dOCLCQ$dTEF$dOCLCQ$dMMU$dOHX$dBTCTA$dYDXCP$dOCLCO$dCIT$dDLC
042 $alccopycat
050 00 $aQP551$b.P69576 2014
072 7 $aQP$2lcco
082 04 $a570.3
245 00 $aProtein conformational dynamics /$cKe-li Han, Xin Zhang, Ming-jun Yang, editors.
264 1 $aCham ;$aNew York :$bSpringer,$c[2014]
264 4 $c©2014
300 $axii, 488 pages :$billustrations (some color) ;$c24 cm.
336 $atext$btxt$2rdacontent
337 $aunmediated$bn$2rdamedia
338 $avolume$bnc$2rdacarrier
490 1 $aAdvances in experimental medicine & biology,$x0065-2598 ;$vvolume 805
520 $a"This book discusses how biological molecules exert their function and regulate biological processes, with a clear focus on how conformational dynamics of proteins are critical in this respect. In the last decade, the advancements in computational biology, nuclear magnetic resonance including paramagnetic relaxation enhancement, and fluorescence-based ensemble/single-molecule techniques have shown that biological molecules (proteins, DNAs and RNAs) fluctuate under equilibrium conditions. The conformational and energetic spaces that these fluctuations explore likely contain active conformations that are critical for their function. More interestingly, these fluctuations can respond actively to external cues, which introduces layers of tight regulation on the biological processes that they dictate. A growing number of studies have suggested that conformational dynamics of proteins govern their role in regulating biological functions, examples of this regulation can be found in signal transduction, molecular recognition, apoptosis, protein / ion / other molecules translocation and gene expression"--$cPublisher's description.
504 $aIncludes bibliographical references and index.
505 0 $aProtein folding simulations by generalized-ensemble algorithms -- Application of Markov state models to simulate long timescale dynamics of biological macromolecules -- Understanding protein dynamics using conformational ensembles -- Generative models of conformational dynamics -- Generalized spring tensor models for protein fluctuation dynamics and conformational changes -- The joys and perils of flexible fitting -- Coarse-grained models of the proteins backbone conformational dynamics -- Simulating protein folding in different environmental conditions -- Simulating the peptide folding kinetic related spectra based on the Markov state model -- The dilemma of conformational dynamics in enzyme catalysis: perspectives from theory and experiment -- Exploiting intrinsic flexibility in drug design -- NMR and computational methods in the structural and dynamic characterization of ligand-receptor interactions -- Molecular dynamics simulation of membrane proteins -- Free-energy landscape of intrinsically disordered proteins investigated by all-atom multicanonical molecular dynamics -- Coordination and control inside simple biomolecular machines -- Multi-state targeting machinery govern the fidelity and efficiency of protein localization -- Molecular dynamics simulations of F₁-ATPase -- Chemosensorial G-proteins-coupled receptors: a perspective from computational methods.
650 0 $aProteins$xConformation.
650 0 $aBiology.
650 12 $aProtein Conformation.
700 1 $aHan, Ke-Li,$eeditor of compilation.
700 1 $aZhang, Xin,$d1978-$eeditor of compilation.
700 1 $aYang, Ming-jun,$eeditor of compilation.
776 08 $iOnline version:$tProtein conformational dynamics.$dCham ; New York : Springer, 2014$z9783319029702$w(OCoLC)873822128
830 0 $aAdvances in experimental medicine and biology ;$v805.$x0065-2598
856 42 $3Publisher description$uhttp://www.loc.gov/catdir/enhancements/fy1405/2014930165-d.html
856 41 $3Table of contents only$uhttp://www.loc.gov/catdir/enhancements/fy1405/2014930165-t.html