LEADER 04894nam 2201081z- 450 001 9910557371103321 005 20231214132937.0 035 $a(CKB)5400000000042180 035 $a(oapen)https://directory.doabooks.org/handle/20.500.12854/76965 035 $a(EXLCZ)995400000000042180 100 $a20202201d2021 |y 0 101 0 $aeng 135 $aurmn|---annan 181 $ctxt$2rdacontent 182 $cc$2rdamedia 183 $acr$2rdacarrier 200 10$aThe Conformational Universe of Proteins and Peptides: Tales of Order and Disorder 210 $aBasel, Switzerland$cMDPI - Multidisciplinary Digital Publishing Institute$d2021 215 $a1 electronic resource (230 p.) 311 $a3-0365-2352-9 311 $a3-0365-2351-0 330 $aProteins represent one of the most abundant classes of biological macromolecules and play crucial roles in a vast array of physiological and pathological processes. The knowledge of the 3D structure of a protein, as well as the possible conformational transitions occurring upon interaction with diverse ligands, are essential to fully comprehend its biological function.In addition to globular, well-folded proteins, over the past few years, intrinsically disordered proteins (IDPs) have received a lot of attention. IDPs are usually aggregation-prone and may form toxic amyloid fibers and oligomers associated with several human pathologies. Peptides are smaller in size than proteins but similarly represent key elements of cells. A few peptides are able to work as tumor markers and find applications in the diagnostic and therapeutic fields. The conformational analysis of bioactive peptides is important to design novel potential drugs acting as selective modulators of specific receptors or enzymes. Nevertheless, synthetic peptides reproducing different protein fragments have frequently been implemented as model systems in folding studies relying on structural investigations in water and/or other environments.This book contains contributions (seven original research articles and five reviews published in the journal Molecules) on the above-described topics and, in detail, it includes structural studies on globular folded proteins, IDPs and bioactive peptides. These works were conducted usingdifferent experimental methods. 517 $aConformational Universe of Proteins and Peptides 606 $aResearch & information: general$2bicssc 610 $amass spectrometric epitope mapping 610 $agas phase immune complex dissociation 610 $aapparent gas phase dissociation constants 610 $aapparent gas phase activation energies 610 $aITEM-TWO 610 $anative mass spectrometry 610 $aTRIOBP 610 $acancer 610 $adeafness 610 $ahearing loss 610 $amental illness 610 $aschizophrenia 610 $aactin 610 $acytoskeleton 610 $adisordered structure 610 $aprotein aggregation 610 $asolid-state NMR 610 $aELDOR-detected NMR 610 $aATP hydrolysis 610 $aATP analogues 610 $aDnaB helicase 610 $aABC transporter 610 $abiopesticides 610 $aantifungal activity 610 $ainsecticidal activity 610 $amechanism of action 610 $atransgenic crops 610 $aprotein folding 610 $aNMR 610 $aHigh Hydrostatic Pressure 610 $aACE2 610 $aviral spike receptor-binding domain 610 $aSARS-CoV-2 610 $atransmission 610 $abioinformatics 610 $aIDP 1 610 $abinding 2 610 $amolecular dynamics 3 610 $aMELD×MD 4 610 $aadvanced sampling 5 610 $ap53 6 610 $aMDM2 7 610 $aNAD(P)H-dependent oxidoreductase 610 $azinc-containing alcohol dehydrogenase 610 $acofactor binding and release 610 $ainterdomain cleft dynamics 610 $amolecular dynamics simulations 610 $adenatured state ensemble 610 $aprotein coil library 610 $apeptides 610 $aintrinsically disordered proteins 610 $aion-pairing interaction 610 $aside-chain length 610 $acharged amino acids 610 $a?-hairpin 610 $apeptide 610 $aFriedman's test 610 $abackbone atom coordinate variances and uncertainties 610 $asuperimposition 610 $ananobody 610 $aprotein structure 610 $aimmunoglobulin domain 615 7$aResearch & information: general 700 $aLeone$b Marilisa$4edt$01307052 702 $aLeone$b Marilisa$4oth 906 $aBOOK 912 $a9910557371103321 996 $aThe Conformational Universe of Proteins and Peptides: Tales of Order and Disorder$93028659 997 $aUNINA