Počet záznamů: 1
Structure of the ordered hydration of amino acids in proteins: analysis of crystal structures
- 1.
SYSNO ASEP 0457403 Druh ASEP J - Článek v odborném periodiku Zařazení RIV J - Článek v odborném periodiku Poddruh J Článek ve WOS Název Structure of the ordered hydration of amino acids in proteins: analysis of crystal structures Tvůrce(i) Biedermannová, Lada (BTO-N) RID, ORCID
Schneider, Bohdan (BTO-N) RID, ORCIDZdroj.dok. Acta Crystallographica Section D-Biological Crystallography. - : Oxford Blackwell - ISSN 1399-0047
Roč. 71, č. 11 (2015), s. 2178-2202Poč.str. 25 s. Jazyk dok. eng - angličtina Země vyd. GB - Velká Británie Klíč. slova protein hydration ; structural biology ; X-ray crystallography Vědní obor RIV EB - Genetika a molekulární biologie Obor OECD Biochemistry and molecular biology Způsob publikování Open access Institucionální podpora BTO-N - RVO:86652036 UT WOS 000468874000002 DOI 10.1107/S1399004715015679 Anotace Crystallography provides unique information about the arrangement of water molecules near protein surfaces. Using a nonredundant set of 2818 protein crystal structures with a resolution of better than 1.8 angstrom, the extent and structure of the hydration shell of all 20 standard amino-acid residues were analyzed as function of the residue conformation, secondary structure and solvent accessibility. The results show how hydration depends on the amino-acid conformation and the environment in which it occurs. After conformational clustering of individual residues, the density distribution of water molecules was compiled and the preferred hydration sites were determined as maxima in the pseudo-electron-density representation of water distributions. Many hydration sites interact with both main-chain and side-chain amino-acid atoms, and several occurrences of hydration sites with less canonical contacts, such as carbon-donor hydrogen bonds, OH-pi interactions and off-plane interactions with aromatic heteroatoms, are also reported. Information about the location and relative importance of the empirically determined preferred hydration sites in proteins has applications in improving the current methods of hydration-site prediction in molecular replacement, ab initio protein structure prediction and the set-up of molecular-dynamics simulations. Pracoviště Biotechnologický ústav Kontakt Monika Kopřivová, Monika.Koprivova@ibt.cas.cz, Tel.: 325 873 700 Rok sběru 2016 Elektronická adresa http://journals.iucr.org/d/issues/2015/11/00/dw5143/index.html
Počet záznamů: 1