Pub Date : 2000-03-01DOI: 10.1016/S0307-4412(99)00130-2
Peter Grunwald
A series of simple, low-cost experiments is described in this paper that allows students to be introduced to some basic kinetic laws relating to heterogeneous catalysis. Immobilized yeast cells are used as the example and therefore simultaneously offer the opportunity to acquaint the students with the theoretical and practical background of an important branch of biotechnology.
{"title":"Experimental treatment of the laws of heterogeneous catalysis with immobilized yeast cells (Saccharomyces cerevisiae)","authors":"Peter Grunwald","doi":"10.1016/S0307-4412(99)00130-2","DOIUrl":"10.1016/S0307-4412(99)00130-2","url":null,"abstract":"<div><p>A series of simple, low-cost experiments is described in this paper that allows students to be introduced to some basic kinetic laws relating to heterogeneous catalysis. Immobilized yeast cells are used as the example and therefore simultaneously offer the opportunity to acquaint the students with the theoretical and practical background of an important branch of biotechnology.</p></div>","PeriodicalId":80258,"journal":{"name":"Biochemical education","volume":"28 2","pages":"Pages 96-99"},"PeriodicalIF":0.0,"publicationDate":"2000-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0307-4412(99)00130-2","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"56624022","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2000-03-01DOI: 10.1016/S0307-4412(99)00083-7
Roberto Gambari
Here, we report a simple experimental approach for demonstrating sequence-selectivity of DNA-binding drugs by using the polymerase-chain reaction (PCR). The experiments described could be easily and reproducibly performed by medical and science students and biochemistry teachers, do not require complex or expensive instruments and 32P labelled probes or primers. The procedure described could represent a novel approach to practical biochemistry teaching in the field of biochemical pharma-cology.
{"title":"A guided experimental approach to practical molecular pharmacology teaching: demonstration of sequence selectivity of DNA-binding drugs by arrested polymerase chain reaction","authors":"Roberto Gambari","doi":"10.1016/S0307-4412(99)00083-7","DOIUrl":"10.1016/S0307-4412(99)00083-7","url":null,"abstract":"<div><p>Here, we report a simple experimental approach for demonstrating sequence-selectivity of DNA-binding drugs by using the polymerase-chain reaction (PCR). The experiments described could be easily and reproducibly performed by medical and science students and biochemistry teachers, do not require complex or expensive instruments and <sup>32</sup>P labelled probes or primers. The procedure described could represent a novel approach to practical biochemistry teaching in the field of biochemical pharma-cology.</p></div>","PeriodicalId":80258,"journal":{"name":"Biochemical education","volume":"28 2","pages":"Pages 100-103"},"PeriodicalIF":0.0,"publicationDate":"2000-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0307-4412(99)00083-7","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"56623549","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2000-03-01DOI: 10.1016/S0307-4412(99)00127-2
Brian N. Blanchette, Bal Ram Singh
The unique bio-analytical properties of the amino acid tyrosine (Tyr) are the focus of this experiment from the research oriented biochemistry laboratory course at our university. In the present study pKa1, pKa2, and pKa3 values for free Tyr were estimated to be 2.30, 9.40, and 9.97, respectively, when free Tyr was titrated with 1 mM NaOH and 1 mM HCl using a pH meter. Spectrophotometric analysis of the phenolic side chain pKa3 revealed a value of 10.14, which was consistent with the pKas estimated from the pH meter. The results from this experiment will allow students to compare the free Tyr properties with those present in a protein.
{"title":"A single protein research integrated advanced biochemistry laboratory course; spectroscopic determination of tyrosyl side chain pKa","authors":"Brian N. Blanchette, Bal Ram Singh","doi":"10.1016/S0307-4412(99)00127-2","DOIUrl":"https://doi.org/10.1016/S0307-4412(99)00127-2","url":null,"abstract":"<div><p>The unique bio-analytical properties of the amino acid tyrosine (Tyr) are the focus of this experiment from the research oriented biochemistry laboratory course at our university. In the present study p<em>K</em><sub>a<sub>1</sub></sub>, p<em>K</em><sub>a<sub>2</sub></sub>, and p<em>K</em><sub>a<sub>3</sub></sub> values for free Tyr were estimated to be 2.30, 9.40, and 9.97, respectively, when free Tyr was titrated with 1<!--> <!-->mM NaOH and 1<!--> <!-->mM HCl using a pH meter. Spectrophotometric analysis of the phenolic side chain p<em>K</em><sub>a<sub>3</sub></sub> revealed a value of 10.14, which was consistent with the p<em>K</em><sub>a</sub><em>s</em> estimated from the pH meter. The results from this experiment will allow students to compare the free Tyr properties with those present in a protein.</p></div>","PeriodicalId":80258,"journal":{"name":"Biochemical education","volume":"28 2","pages":"Pages 107-109"},"PeriodicalIF":0.0,"publicationDate":"2000-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0307-4412(99)00127-2","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"137439794","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Here, we report a simple experimental approach for demonstrating sequence-selectivity of DNA-binding drugs by using the polymerase-chain reaction (PCR). The experiments described could be easily and reproducibly performed by medical and science students and biochemistry teachers, do not require complex or expensive instruments and 32P labelled probes or primers. The procedure described could represent a novel approach to practical biochemistry teaching in the field of biochemical pharma-cology.
{"title":"A guided experimental approach to practical molecular pharmacology teaching: demonstration of sequence selectivity of DNA-binding drugs by arrested polymerase chain reaction.","authors":"Gambari","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Here, we report a simple experimental approach for demonstrating sequence-selectivity of DNA-binding drugs by using the polymerase-chain reaction (PCR). The experiments described could be easily and reproducibly performed by medical and science students and biochemistry teachers, do not require complex or expensive instruments and 32P labelled probes or primers. The procedure described could represent a novel approach to practical biochemistry teaching in the field of biochemical pharma-cology.</p>","PeriodicalId":80258,"journal":{"name":"Biochemical education","volume":"28 2","pages":"100-103"},"PeriodicalIF":0.0,"publicationDate":"2000-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"21575436","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2000-03-01DOI: 10.1016/S0307-4412(99)00138-7
Gareth Denyer
This paper describes an easy method for empowering biochemistry students to think critically about research data. The technique encourages students to formulate their own opinions by removing the usually dominant ‘expert’ commentary. The exercise can be done individually or in very large groups, requires no specialist materials and confirmation that articulation and criticism skills have been learnt can be assessed under standard examination conditions. The skills learnt are not discipline specific and, as well as learning how best to read research papers, students also learn something about the research process.
{"title":"Strategies for building criticism skills in undergraduate biochemists","authors":"Gareth Denyer","doi":"10.1016/S0307-4412(99)00138-7","DOIUrl":"10.1016/S0307-4412(99)00138-7","url":null,"abstract":"<div><p>This paper describes an easy method for empowering biochemistry students to think critically about research data. The technique encourages students to formulate their own opinions by removing the usually dominant ‘expert’ commentary. The exercise can be done individually or in very large groups, requires no specialist materials and confirmation that articulation and criticism skills have been learnt can be assessed under standard examination conditions. The skills learnt are not discipline specific and, as well as learning how best to read research papers, students also learn something about the research process.</p></div>","PeriodicalId":80258,"journal":{"name":"Biochemical education","volume":"28 2","pages":"Pages 74-75"},"PeriodicalIF":0.0,"publicationDate":"2000-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0307-4412(99)00138-7","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"21575531","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2000-03-01DOI: 10.1016/S0307-4412(99)00135-1
Mona L. Hall, Adele J. Wolfson
After purification of lysozyme, our biochemistry students write a research proposal that outlines a strategy for studying this enzyme after alteration by site-directed mutagenesis. Despite a literature search that yielded a wealth of background information, students were often overwhelmed by the assignment because they were not familiar with advanced techniques of protein analysis. We therefore developed a series of journal clubs in which teams of students present methods and data found in papers dealing with lysozyme. The five topics for journal clubs include; substrate binding and mechanism; spectroscopic techniques; stability analysis; two-dimensional NMR; and X-ray crystallography. After the adoption of the group talks, the quality of the research proposals improved immensely and students found the assignment to be an educationally rewarding exercise.
{"title":"Journal club as a supplement to the undergraduate biochemistry laboratory","authors":"Mona L. Hall, Adele J. Wolfson","doi":"10.1016/S0307-4412(99)00135-1","DOIUrl":"https://doi.org/10.1016/S0307-4412(99)00135-1","url":null,"abstract":"<div><p>After purification of lysozyme, our biochemistry students write a research proposal that outlines a strategy for studying this enzyme after alteration by site-directed mutagenesis. Despite a literature search that yielded a wealth of background information, students were often overwhelmed by the assignment because they were not familiar with advanced techniques of protein analysis. We therefore developed a series of journal clubs in which teams of students present methods and data found in papers dealing with lysozyme. The five topics for journal clubs include; substrate binding and mechanism; spectroscopic techniques; stability analysis; two-dimensional NMR; and X-ray crystallography. After the adoption of the group talks, the quality of the research proposals improved immensely and students found the assignment to be an educationally rewarding exercise.</p></div>","PeriodicalId":80258,"journal":{"name":"Biochemical education","volume":"28 2","pages":"Pages 71-73"},"PeriodicalIF":0.0,"publicationDate":"2000-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0307-4412(99)00135-1","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"91634921","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Several mitochondrial fractions were screened for suitability in practical experiments designed for students, with the following issues in mind: avoiding the use of animals; minimal expenditure of labour and time; high enzyme activities; accessible instruments and low-cost materials. Turnips and potato tubers were identified as the best materials from which to extract purified mitochondria according to these criteria, with high respiratory activities and integrity maintained during five consecutive days. Mitochondrial respiration was assayed for succinate, exogenous NADH, malate/pyruvate and alpha-ketoglutarate oxidations with excellent results. At the fifth day, the respiratory control was still about 3, the integrity of the outer mitochondrial membrane maintained at values higher than 80%, and the enzymes retained more than 55% of the initial activities.
{"title":"The excellence of turnip mitochondrial fraction.","authors":"Vicente, Madeira","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Several mitochondrial fractions were screened for suitability in practical experiments designed for students, with the following issues in mind: avoiding the use of animals; minimal expenditure of labour and time; high enzyme activities; accessible instruments and low-cost materials. Turnips and potato tubers were identified as the best materials from which to extract purified mitochondria according to these criteria, with high respiratory activities and integrity maintained during five consecutive days. Mitochondrial respiration was assayed for succinate, exogenous NADH, malate/pyruvate and alpha-ketoglutarate oxidations with excellent results. At the fifth day, the respiratory control was still about 3, the integrity of the outer mitochondrial membrane maintained at values higher than 80%, and the enzymes retained more than 55% of the initial activities.</p>","PeriodicalId":80258,"journal":{"name":"Biochemical education","volume":"28 2","pages":"104-106"},"PeriodicalIF":0.0,"publicationDate":"2000-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"21575437","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2000-03-01DOI: 10.1111/J.1539-3429.2000.TB00034.X
Vicente, Madeira
Several mitochondrial fractions were screened for suitability in practical experiments designed for students, with the following issues in mind: avoiding the use of animals; minimal expenditure of labour and time; high enzyme activities; accessible instruments and low-cost materials. Turnips and potato tubers were identified as the best materials from which to extract purified mitochondria according to these criteria, with high respiratory activities and integrity maintained during five consecutive days. Mitochondrial respiration was assayed for succinate, exogenous NADH, malate/pyruvate and alpha-ketoglutarate oxidations with excellent results. At the fifth day, the respiratory control was still about 3, the integrity of the outer mitochondrial membrane maintained at values higher than 80%, and the enzymes retained more than 55% of the initial activities.
{"title":"The excellence of turnip mitochondrial fraction.","authors":"Vicente, Madeira","doi":"10.1111/J.1539-3429.2000.TB00034.X","DOIUrl":"https://doi.org/10.1111/J.1539-3429.2000.TB00034.X","url":null,"abstract":"Several mitochondrial fractions were screened for suitability in practical experiments designed for students, with the following issues in mind: avoiding the use of animals; minimal expenditure of labour and time; high enzyme activities; accessible instruments and low-cost materials. Turnips and potato tubers were identified as the best materials from which to extract purified mitochondria according to these criteria, with high respiratory activities and integrity maintained during five consecutive days. Mitochondrial respiration was assayed for succinate, exogenous NADH, malate/pyruvate and alpha-ketoglutarate oxidations with excellent results. At the fifth day, the respiratory control was still about 3, the integrity of the outer mitochondrial membrane maintained at values higher than 80%, and the enzymes retained more than 55% of the initial activities.","PeriodicalId":80258,"journal":{"name":"Biochemical education","volume":"28 2 1","pages":"104-106"},"PeriodicalIF":0.0,"publicationDate":"2000-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1111/J.1539-3429.2000.TB00034.X","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"63148007","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2000-03-01DOI: 10.1016/S0307-4412(99)00144-2
Christopher A Smith
This article emphasizes the importance of getting students to understand the ways in which polypeptides fold to form protein molecules with complex higher-ordered structures. Modern views on how this folding occurs in vitro and in the cell are summarized and set within an appropriate biological context.
{"title":"How do proteins fold?","authors":"Christopher A Smith","doi":"10.1016/S0307-4412(99)00144-2","DOIUrl":"https://doi.org/10.1016/S0307-4412(99)00144-2","url":null,"abstract":"<div><p>This article emphasizes the importance of getting students to understand the ways in which polypeptides fold to form protein molecules with complex higher-ordered structures. Modern views on how this folding occurs in vitro and in the cell are summarized and set within an appropriate biological context.</p></div>","PeriodicalId":80258,"journal":{"name":"Biochemical education","volume":"28 2","pages":"Pages 76-79"},"PeriodicalIF":0.0,"publicationDate":"2000-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0307-4412(99)00144-2","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"90002194","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
The unique bio-analytical properties of the amino acid tyrosine (Tyr) are the focus of this experiment from the research oriented biochemistry laboratory course at our university. In the present study pK(a(1)), pK(a(2)), and pK(a(3)) values for free Tyr were estimated to be 2.30, 9.40, and 9.97, respectively, when free Tyr was titrated with 1mM NaOH and 1mM HCl using a pH meter. Spectrophotometric analysis of the phenolic side chain pK(a(3)) revealed a value of 10.14, which was consistent with the pK(a)s estimated from the pH meter. The results from this experiment will allow students to compare the free Tyr properties with those present in a protein.
{"title":"A single protein research integrated advanced biochemistry laboratory course; spectroscopic determination of tyrosyl side chain pKa.","authors":"Blanchette, Singh","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>The unique bio-analytical properties of the amino acid tyrosine (Tyr) are the focus of this experiment from the research oriented biochemistry laboratory course at our university. In the present study pK(a(1)), pK(a(2)), and pK(a(3)) values for free Tyr were estimated to be 2.30, 9.40, and 9.97, respectively, when free Tyr was titrated with 1mM NaOH and 1mM HCl using a pH meter. Spectrophotometric analysis of the phenolic side chain pK(a(3)) revealed a value of 10.14, which was consistent with the pK(a)s estimated from the pH meter. The results from this experiment will allow students to compare the free Tyr properties with those present in a protein.</p>","PeriodicalId":80258,"journal":{"name":"Biochemical education","volume":"28 2","pages":"107-109"},"PeriodicalIF":0.0,"publicationDate":"2000-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"21575438","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}