| NKED79 | Interactions in Biomolecular Systems, 15 ECTS credits. /Biomolekylär växelverkan/ |
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Prel. scheduled
hours: 120 |
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Area of Education: Science Subject area: Chemistry |
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| Advancement level
(A-D): D
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| Aim: The course goal is to give the students a deep knowledge about structure/function relations in bio-molecular systems. Special emphasis is put on bio-molecular interactions and on molecular mechanisms in enzymatic catalysis. After the course the student is expected to: �Y Master important methods and theories that describe dynamics in bio-molecular systems �Y Master central concepts and theories for molecular interactions and for reaction mechanisms �Y Have good skills to communicate bioorganic research problems, methods and results �Y Have the ability to critically read advanced literature within the field. |
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| Prerequisites: (valid for students admitted to programmes within which the course is offered) Admittance to the course requires that the course Biochemistry 2 is approved or corresponding knowledge. Note: Admission requirements for non-programme students usually also include admission requirements for the programme and threshhold requirements for progression within the programme, or corresponding. |
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| Organisation: The course will contain a mix of lectures, demonstrations, student led seminars and laboratory work. All educational subsections are compulsory. |
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| Course contents: A. The course includes theory on: *Bio-molecular dynamics, *Analysis of complex kinetics and identification of intermediates, *Enzymatic catalysis including the relations between the organisation of the active site and the catalytic activity, *Interactions between enzyme and substrate with emphasis on electrostatic and hydrophobic effects, *Inhibitors and their structure and function, *Co-operativity and allostery, *Stereospecificity in enzymatic reactions and their origin, *Specificity and editing in biosynthesis of macromolecules, *Use of recombinant DNA-technology in the study of bio-molecular interactions, *Conformational stability of proteins and the kinetics of protein folding. B. The section on molecular modelling includes use of software for use molecular dynamics in the studies of bio-molecules and their interactions with substrates. C. The laboratory work is interwoven with the lectures on molecular modelling. |
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| Course literature: �?oStructure and mechanism in protein science, a guide to enzyme catalysis and protein folding�?� by A. Fersht. Publisher: W.H. Freeman and Company. ISBN 0-7167-3268-8 |
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| Examination: | |||
| Written examination |
10 p |
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Course language is . Department offering the course: IFM. Director of Studies: Stefan Svensson Examiner: Nalle Jonsson Course Syllabus in Swedish |
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