The dimension of certain tree structures is of importance in percolation theory, as well as in the theoretical treatment of many other branching processes. We present a method of determining the Hausdorff dimension of such structures by employing the technique of Mauldin and Williams. The dimension is calculated based on the probability of generation of each branch from its parent on the tree representing the process. We use this method to analyze the dimension of tree structures representing two-directional linear bonding between equally weighted monomers, and show how it can be used to model enzymatic reaction pathways.

(1991). The Knowledge and Pedagogical Base of Science Education: An Overview. Teaching Education: Vol. 3, No. 2, pp. 11-16.

ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTPermeable membrane/mass spectrometric measurement of solvent proton/deuterium, carbon-12/carbon-13, and oxygen-16/oxygen-18 kinetic isotope effects associated with .alpha.-chymotrypsin deacylation: evidence for reaction mechanism plasticityAwadhesh K. Mishra and Michael H. KlapperCite this: Biochemistry 1986, 25, 23, 7328–7336Publication Date (Print):November 18, 1986Publication History Published online1 May 2002Published inissue 18 November 1986https://pubs.acs.org/doi/10.1021/bi00371a014https://doi.org/10.1021/bi00371a014research-articleACS PublicationsRequest reuse permissionsArticle Views54Altmetric-Citations4LEARN ABOUT THESE METRICSArticle Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days.Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts.The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the Altmetric Attention Score and how the score is calculated. Share Add toView InAdd Full Text with ReferenceAdd Description ExportRISCitationCitation and abstractCitation and referencesMore Options Share onFacebookTwitterWechatLinked InRedditEmail Other access optionsGet e-Alertsclose Get e-Alerts

ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTReactivity of protein histidines toward the hydrated electronJerald P. Steiner, M. Faraggi, Michael H. Klapper, and Leon DorfmanCite this: Biochemistry 1985, 24, 9, 2139–2146Publication Date (Print):April 1, 1985Publication History Published online1 May 2002Published inissue 1 April 1985https://pubs.acs.org/doi/10.1021/bi00330a006https://doi.org/10.1021/bi00330a006research-articleACS PublicationsRequest reuse permissionsArticle Views65Altmetric-Citations6LEARN ABOUT THESE METRICSArticle Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days.Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts.The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the Altmetric Attention Score and how the score is calculated. Share Add toView InAdd Full Text with ReferenceAdd Description ExportRISCitationCitation and abstractCitation and referencesMore Options Share onFacebookTwitterWechatLinked InRedditEmail Other access optionsGet e-Alertsclose Get e-Alerts

The formate radical (CO2-) reacts with ribonuclease A to form the cystine disulfide radical as one of the products. CO2- reacts with the riboflavin binding protein of chicken egg white with the ultimate product being the neutral flavin semiquinone. Formation of the disulfide radical in ribonuclease is slower than the reaction between protein and CO2-; formation of the flavin semiquinone in the riboflavin binding protein is slower than the protein-CO2- reaction. We conclude for both proteins that CO2- must reduce an as yet unidentified group or groups, which in turn reduce(s) the disulfide of RNase or the flavin of riboflavin binding protein. This conclusion is supported in the case of ribonuclease by the observation of a transient, broad absorption band centered between 350 and 370 nm. The CO2--initiated reductions of the disulfide in ribonuclease and the flavin in the riboflavin binding protein are mixed first- and second-order processes. We propose that the transfer of an electron from the unknown intermediate(s) to the final product involves both inter- and intramolecular paths between groups that may not be in van der Waals contact. With the hydrated electron, in contrast to CO2-, as reductant of the riboflavin binding protein, the anionic semiquinone is observed as an intermediate. The anionic semiquinone is then rapidly protonated, yielding the stable neutral semiquinone. From the reaction kinetics and protein concentration dependence, we conclude that a group or groups on the protein donate(s) a proton to the anionic semiquinone by both inter- and intramolecular paths.

Daunorubicin aqueous solutions were reduced by COO.−1 or eaq −1 free radicals produced by pulse radiolysis. The kinetics of the semiquinone radical formation and decay were studied. The semiquinone disproportionation leads to a pseudo‐equilibrium between the drug, its semiquinone and hydroquinone reduced states (K eq = 30 at pH 7), which lasts a few hunderd milliseconds and which is destroyed by the hydroquinone glycosidic cleavage. Consequences concerning daunorubicin antitumour action are briefly discussed.

Chemischer InformationsdienstVolume 11, Issue 18 Preparative Organic Chemistry ChemInform Abstract: A NOVEL OXYGEN-18 KINETIC ISOTOPE EFFECT IN AN α-CHYMOTRYPSIN CATALYZED TRANSESTERIFICATION C.-L. A. WANG, C.-L. A. WANGSearch for more papers by this authorC. M. TROUT, C. M. TROUTSearch for more papers by this authorK. C. CALVO, K. C. CALVOSearch for more papers by this authorM. H. KLAPPER, M. H. KLAPPERSearch for more papers by this authorL. K. WONG, L. K. WONGSearch for more papers by this author C.-L. A. WANG, C.-L. A. WANGSearch for more papers by this authorC. M. TROUT, C. M. TROUTSearch for more papers by this authorK. C. CALVO, K. C. CALVOSearch for more papers by this authorM. H. KLAPPER, M. H. KLAPPERSearch for more papers by this authorL. K. WONG, L. K. WONGSearch for more papers by this author First published: May 6, 1980 https://doi.org/10.1002/chin.198018086AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onFacebookTwitterLinkedInRedditWechat No abstract is available for this article. Volume11, Issue18May 6, 1980 RelatedInformation

Gametes of a predominately male hybrid Allomyces produce a low molecular weight substance which appears to inhibit the response of the male cells to the female chemotactic agent sirenin. A partial purification of this inhibitor, which we call keerosin, involves gel exclusion and silicic acid column chromatography.

Chemischer InformationsdienstVolume 4, Issue 4 Natural Products ChemInform Abstract: ELEKTROCHEMISCHE UNTERSUCHUNGEN VON HAEMOPROTEINEN, COULOMETRISCHE, POLAROGRAPHISCHE UND KOMBINIERTE SPEKTROELEKTROCHEMISCHE METHODEN BEI DER RED. VON HAEMOPROSTHETISCHEN GRUPPEN IN CYTOCHROM C STEPHEN R. BETSO, STEPHEN R. BETSOSearch for more papers by this authorMICHAEL H. KLAPPER, MICHAEL H. KLAPPERSearch for more papers by this authorLARRY B. ANDERSON, LARRY B. ANDERSONSearch for more papers by this author STEPHEN R. BETSO, STEPHEN R. BETSOSearch for more papers by this authorMICHAEL H. KLAPPER, MICHAEL H. KLAPPERSearch for more papers by this authorLARRY B. ANDERSON, LARRY B. ANDERSONSearch for more papers by this author First published: January 23, 1973 https://doi.org/10.1002/chin.197304429AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onFacebookTwitterLinked InRedditWechat No abstract is available for this article. Volume4, Issue4January 23, 1973 RelatedInformation

This chapter discusses the hybridization of chemically modified proteins. For successful hybridization experiments, the variant proteins must have sufficiently different electrophoretic mobilities. The variants commonly used are isolated from natural sources. There are proteins, however, for which such variant isolation is not feasible. In these cases, a charge alteration may be artificially introduced by chemical means. Protein modification with succinic anhydride can provide the necessary chemically modified species. Hybridization of succinylated protein with unmodified protein has been used to detect association-dissociation equilibrium in an oligomeric protein and to determine the number of subunits in an oligomer. The modified protein should have an electrophoretic mobility substantially different from that of the native protein. The quaternary structures of modified and native protein must be identical and the altered enzyme must be reconstitutable after dissociation.

This chapter discusses acylation with dicarboxylic acid anhydrides. Succinic and maleic anhydride, or analogs of these two compounds, is utilized in a variety of protein modification studies. During the course of the reaction most of the anhydride is hydrolyzed. The dicarboxylic acid side product may be separated from the modified protein by dialysis, by passage through a column of anion exchange resin (for example, Amberlite IRA-400 in the chloride form), or by gel exclusion chromatography (for example, with Sephadex G-25). The stability of the half amide adduct depends on the anhydride used in the reaction. Five purposes for which the dicarboxylic anhydrides have been utilized are discussed in the chapter, which include protein dissociation, protein hybridization, mapping of lysine peptides, peptide sequencing, lysine side-chain reactivity and function, and introduction of new functional groups. The relatively high specificity of succinic and maleic anhydride for primary amino groups suggests that these reagents may be useful for studying the reactivities of lysine side chains and for elucidating the roles these residues may play in the biological activities of proteins.

ADVERTISEMENT RETURN TO ISSUEPREVCommentaryNEXTTruth and aesthetics in chemistryMichael H. Klapper Cite this: J. Chem. Educ. 1969, 46, 9, 577Publication Date (Print):September 1, 1969Publication History Received3 August 2009Published online1 September 1969Published inissue 1 September 1969https://doi.org/10.1021/ed046p577Request reuse permissions This publication is free to access through this site. Learn MoreArticle Views286Altmetric-Citations1LEARN ABOUT THESE METRICSArticle Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days.Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts.The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the Altmetric Attention Score and how the score is calculated. Share Add toView InAdd Full Text with ReferenceAdd Description ExportRISCitationCitation and abstractCitation and referencesMore Options Share onFacebookTwitterWechatLinked InReddit PDF (3 MB) Get e-Alertsclose Get e-Alerts