Education + training . Volume 50, Number 1 50th anniversary commemorative issue [[electronic resource]]

• Record Nr.: UNINA9910784754503321
• Pubbl/distr/stampa: [Bradford, England], : Emerald, 2008
• ISBN: 1-281-38502-6; 9786611385026; 1-84663-803-8
• Descrizione fisica: 1 online resource (86 p.)
• Collana: Education & training ; ; v. 50, no. 1
• Disciplina: 600
• Soggetti: Technical education - Great Britain; Technical education
• Lingua di pubblicazione: Inglese
• Formato: Materiale a stampa
• Livello bibliografico: Monografia
• Note generali: Description based upon print version of record.
• Nota di bibliografia: Includes bibliographical references.
• Nota di contenuto: Cover; CONTENTS; EDITORIAL ADVISORY BOARD; Editorial; Training in British industry; Technical subjects in secondary schools; The work of the careers master; What is an apprentice?; Co-operative training in the Sheffield forging industry; Research in technical colleges; Reflections on 50 years of Education 1 Training; 1958-2008: how access to VET qualifications has changed in Australia; Higher education, the graduate and the labour market: from Robbins to Dearing; The business schools: 50 years on; Revisiting "technical" education; Reflecting on the skills agenda: a construction industry perspectiveCeltic Tiger found in education jungle; Vocational education and training in SMEs; Research news
• Sommario/riassunto: This e-book presents a retrospective look at education over the past 50 years. It contains papers republished from the first issue and a series of viewpoint papers from Editorial Board members reflecting on educational issues over the past 50 years.

Computational approaches to biochemical reactivity [[electronic resource] /] / edited by Gábor Náray-Szabó and Arieh Warshel

• Record Nr.: UNINA9910780037003321
• Pubbl/distr/stampa: Dordrecht ; ; Boston, : Kluwer Academic, c1997
• ISBN: 1-280-20496-6; 9786610204960; 0-306-46934-0
• Edizione: [1st ed. 2002.]
• Descrizione fisica: 1 online resource (392 p.)
• Collana: Understanding chemical reactivity ; ; v. 19
• Altri autori (Persone): Náray-SzabóGábor; WarshelArieh
• Disciplina: 572/.44/015118
• Soggetti: Biochemistry - Mathematical models; Enzyme kinetics; Quantum biochemistry; Ligand binding (Biochemistry) - Mathematical models
• Lingua di pubblicazione: Inglese
• Formato: Materiale a stampa
• Livello bibliografico: Monografia
• Note generali: Description based upon print version of record.
• Nota di bibliografia: Includes bibliographical references and index.
• Nota di contenuto: Quantum Mechanical Models for Reactions in Solution -- Free Energy Perturbation Calculations within Quantum Mechanical Methodologies -- Hybrid Potentials for Molecular Systems in the Condensed Phase -- Molecular Mechanics and Dynamics Simulations of Enzymes -- Electrostatic Interactions in Proteins -- Electrostatic Basis of Enzyme Catalysis -- On the Mechanisms of Proteinases -- Modelling of Proton Transfer Reactions in Enzymes -- Protein-Ligand Interactions.
• Sommario/riassunto: A quantitative description of the action of enzymes and other biological systems is both a challenge and a fundamental requirement for further progress in our und- standing of biochemical processes. This can help in practical design of new drugs and in the development of artificial enzymes as well as in fundamental understanding of the factors that control the activity of biological systems. Structural and biochemical st- ies have yielded major insights about the action of biological molecules and the mechanism of enzymatic reactions. However it is not entirely clear how to use this - portant information in a consistent and quantitative analysis of the factors that are - sponsible for rate ; acceleration in enzyme active sites. The problem is associated with the fact that reaction rates are determined by energetics (i. e. activation energies) and the available experimental methods by themselves cannot provide a correlation - tween structure and energy. Even mutations of specific active site residues, which are extremely useful, cannot tell us about the totality of the interaction between the active site and the substrate. In fact, short of inventing experiments that allow one to measure the forces in enzyme active sites it is hard to see how can one use a direct experimental approach to unambiguously correlate the structure and function of enzymes. In fact, in view of the complexity of biological systems it seems that only computers can handle the task of providing a quantitative structure-function correlation.