The Conformational Universe of Proteins and Peptides: Tales of Order and Disorder

Proteins 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 dive...

Full description

Saved in:
Bibliographic Details
Sonstige:
Year of Publication:2021
Language:English
Physical Description:1 electronic resource (230 p.)
Tags: Add Tag
No Tags, Be the first to tag this record!
LEADER 04729nam-a2201045z--4500
001 993545918804498
005 20231214132937.0
006 m o d
007 cr|mn|---annan
008 202201s2021 xx |||||o ||| 0|eng d
035 |a (CKB)5400000000042180 
035 |a (oapen)https://directory.doabooks.org/handle/20.500.12854/76965 
035 |a (EXLCZ)995400000000042180 
041 0 |a eng 
100 1 |a Leone, Marilisa  |4 edt 
245 1 0 |a The Conformational Universe of Proteins and Peptides: Tales of Order and Disorder 
246 |a Conformational Universe of Proteins and Peptides 
260 |a Basel, Switzerland  |b MDPI - Multidisciplinary Digital Publishing Institute  |c 2021 
300 |a 1 electronic resource (230 p.) 
336 |a text  |b txt  |2 rdacontent 
337 |a computer  |b c  |2 rdamedia 
338 |a online resource  |b cr  |2 rdacarrier 
520 |a Proteins 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. 
546 |a English 
650 7 |a Research & information: general  |2 bicssc 
653 |a mass spectrometric epitope mapping 
653 |a gas phase immune complex dissociation 
653 |a apparent gas phase dissociation constants 
653 |a apparent gas phase activation energies 
653 |a ITEM-TWO 
653 |a native mass spectrometry 
653 |a TRIOBP 
653 |a cancer 
653 |a deafness 
653 |a hearing loss 
653 |a mental illness 
653 |a schizophrenia 
653 |a actin 
653 |a cytoskeleton 
653 |a disordered structure 
653 |a protein aggregation 
653 |a solid-state NMR 
653 |a ELDOR-detected NMR 
653 |a ATP hydrolysis 
653 |a ATP analogues 
653 |a DnaB helicase 
653 |a ABC transporter 
653 |a biopesticides 
653 |a antifungal activity 
653 |a insecticidal activity 
653 |a mechanism of action 
653 |a transgenic crops 
653 |a protein folding 
653 |a NMR 
653 |a High Hydrostatic Pressure 
653 |a ACE2 
653 |a viral spike receptor-binding domain 
653 |a SARS-CoV-2 
653 |a transmission 
653 |a bioinformatics 
653 |a IDP 1 
653 |a binding 2 
653 |a molecular dynamics 3 
653 |a MELD×MD 4 
653 |a advanced sampling 5 
653 |a p53 6 
653 |a MDM2 7 
653 |a NAD(P)H-dependent oxidoreductase 
653 |a zinc-containing alcohol dehydrogenase 
653 |a cofactor binding and release 
653 |a interdomain cleft dynamics 
653 |a molecular dynamics simulations 
653 |a denatured state ensemble 
653 |a protein coil library 
653 |a peptides 
653 |a intrinsically disordered proteins 
653 |a ion-pairing interaction 
653 |a side-chain length 
653 |a charged amino acids 
653 |a β-hairpin 
653 |a peptide 
653 |a Friedman's test 
653 |a backbone atom coordinate variances and uncertainties 
653 |a superimposition 
653 |a nanobody 
653 |a protein structure 
653 |a immunoglobulin domain 
776 |z 3-0365-2352-9 
776 |z 3-0365-2351-0 
700 1 |a Leone, Marilisa  |4 oth 
906 |a BOOK 
ADM |b 2023-12-15 05:36:50 Europe/Vienna  |f system  |c marc21  |a 2022-04-04 09:22:53 Europe/Vienna  |g false 
AVE |i DOAB Directory of Open Access Books  |P DOAB Directory of Open Access Books  |x https://eu02.alma.exlibrisgroup.com/view/uresolver/43ACC_OEAW/openurl?u.ignore_date_coverage=true&portfolio_pid=5338088200004498&Force_direct=true  |Z 5338088200004498  |b Available  |8 5338088200004498