Or exploratory analysis and evaluation. J Comput Chem. 2004;25(13):16052. 85. Humphrey W, Dalke A, Schulten K. VMD: visual molecular dynamics. J Mol Graph. 1996;14(1):33. 278. 86. Pruitt KD, Tatusova T, Brown GR, Maglott DR. NCBI Reference Sequences (RefSeq): present status, new attributes and genome annotation policy. Nucleic Acids Res. 2012;40(Database concern):D130. 87. Altschul SF, Madden TL, Schaffer AA, Zhang J, Zhang Z, Miller W, et al. Gapped BLAST and PSI-BLAST: a brand new generation of protein database search programs. Nucleic Acids Res. 1997;25(17):338902. 88. Edgar RC, Sjolander K. A comparison of scoring functions for protein sequence profile alignment. Bioinformatics. 2004;20(eight):1301. 89. Crooks GE, Hon G, Chandonia JM, Brenner SE. WebLogo: a sequence logo generator. Genome Res. 2004;14(6):11880. 90. Neer EJ, Schmidt CJ, Nambudripad R, Smith TF. The ancient regulatoryprotein family members of WD-repeat proteins. Nature. 1994;371(6495):29700. 91. Smith TF, Gaitatzes C, Saxena K, Neer EJ. The WD repeat: a popular architecture for diverse functions. Trends Biochem Sci. 1999;24(5):181. 92. Ponting CP, Aravind L, Schultz J, Bork P, Koonin EV. Eukaryotic signalling domain homologues in archaea and bacteria. Ancient ancestry and horizontal gene transfer. J Mol Biol. 1999;289(4):7295. 93. Donohue J. Selected topics in hydrogen bonding. In: Wealthy A, Davidson NR, editors. Structural chemistry and molecular biology. San Francisco: W. H. Freeman; 1968. 94. Baker EN, Hubbard RE. Hydrogen bonding in Acs pubs hsp Inhibitors targets globular proteins. Prog Biophys Mol Biol. 1984;44(two):9779. 95. Dehner A, Klein C, Hansen S, Muller L, Buchner J, Schwaiger M, et al. Cooperative binding of p53 to DNA: regulation by protein-protein interactions by way of a double salt bridge. Angew Chem Int Edit. 2005;44(33):52471. 96. Mulkidjanian AY. Conformationally controlled pK-switching in membrane proteins: 1 additional mechanism distinct for the enzyme catalysis FEBS Lett. 1999;463(3):19904.Submit your next manuscript to BioMed Central and take complete advantage of:Practical on the web submission Thorough peer evaluation No space constraints or colour figure charges Quick publication on acceptance Inclusion in PubMed, CAS, Scopus and Google Scholar Study which can be freely out there for redistributionSubmit your manuscript at www.biomedcentral.comsubmitS zJim ez et al. Biotechnol Biofuels (2016) 9:198 DOI 10.1186s130680160615xBiotechnology for BiofuelsOpen AccessRESEARCHRole of surface tryptophan for peroxidase oxidation of nonphenolic ligninVer ica S zJim ez1,2, Jorge Rencoret3, Miguel Angel Rodr uezCarvajal4, Ana Guti rez3, Francisco Javier RuizDue s1 and Angel T. Mart ez1Abstract Background: In spite of claims as key enzymes in enzymatic delignification, 4ebp1 Inhibitors MedChemExpress pretty scarce data on the reaction prices among the ligninolytic versatile peroxidase (VP) and lignin peroxidase (LiP) and the lignin polymer is readily available, due to methodological troubles associated with lignin heterogeneity and low solubility. Outcomes: Two watersoluble sulfonated lignins (from Picea abies and Eucalyptus grandis) have been chemically character ized and used to estimate single electrontransfer prices to the H2O2activated Pleurotus eryngii VP (native enzyme and mutated variant) transient states (compounds I and II bearing two and oneelectron deficiencies, respectively). When the ratelimiting reduction of compound II was quantified by stoppedflow rapid spectrophotometry, from fourfold (softwood lignin) to more than 100fold (hardwood lignin) lower electrontransfe.
