Leo Spyracopoulos

Professor, Faculty of Medicine & Dentistry - Biochemistry Dept

Contact

Professor, Faculty of Medicine & Dentistry - Biochemistry Dept
Email
ls5@ualberta.ca
Phone
(780) 492-2417
Address
416A Medical Sciences Building
8613 - 114 St NW
Edmonton AB
T6G 2H7

Overview

Area of Study / Keywords


About

Dr. Leo Spyracopoulos is currently appointed as Professor in the Department of Biochemistry in the Faculty of Medicine & Dentistry.

Courses

BIOCH 320 - Structure and Catalysis

This course is designed to illustrate, in detail, the relationships between structure and function in biological molecules. It covers: the structure of proteins; experimental techniques used to study proteins; selected illustrations of protein function; enzyme catalysis, kinetics, and regulation; structural carbohydrates and glycobiology; the structure of lipids; biological membranes and mechanisms of transport. Prerequisites: BIOCH 200, CHEM 102 (or SCI 100) and CHEM 263 with a minimum GPA of 2.70 for these three courses. In the case of over-subscription, preference will be given to students enrolled in programs with a requirement for this course.


BIOCH 420 - Proteins: Structure, Function, and Regulation

Principles of protein structure, function, and dynamics, with an introduction to force fields used in modern molecular dynamics. Focus topics include an introduction to intrinsically disordered proteins and their role in misfolding diseases, the structural biology, ligand binding, and mechanisms of membrane bound enzymes, and mechanisms underlying the regulation of protein function and enzymes involved in cell signaling. Prerequisites: BIOCH 320, with a minimum grade of B- or consent of Department. This course is intended for students in Honors or Specialization in Biochemistry. Students in other programs may be admitted subject to availability and with the consent of the Department. Graduate students may not register for credit (see BIOCH 520).


BIOCH 465 - Methods in Molecular Biophysics

Survey of biophysical methods used in the characterization and structural determination of biological macromolecules, from ensemble measurements to single-molecule detection. Topics include mass spectrometry, optical spectroscopy, light microscopy, X-ray and neutron diffraction, electron microscopy, molecular dynamics and nuclear magnetic resonance. Emphasis is on using techniques in evaluating structure-function relationships through the discussion of representative macromolecular systems. Prerequisites: BIOCH 320 with a minimum grade of B- or consent of the Department. This course is intended for students in Honors or Specialization in Biochemistry. Students in other programs may be admitted subject to availability and with the consent of the Department. This course cannot be taken for credit if credit has already been obtained in BIOCH 460.


BIOCH 520 - Protein Chemistry, Structure, and Function

Principles of protein structure, function, and dynamics, with an introduction to force fields used in modern molecular dynamics. Focus topics include an introduction to intrinsically disordered proteins and their role in misfolding diseases, the structural biology, ligand binding, and mechanisms of membrane bound enzymes, and mechanisms underlying the regulation of protein function and enzymes involved in cell signaling. Prerequisites: BIOCH 320, with a minimum grade of B- or consent of Department. Lectures are the same as for BIOCH 420, but with additional assignments and evaluation appropriate to graduate studies. Students in other programs may be admitted subject to availability and with the consent of the Department This course may not be taken for credit if credit has already been obtained in BIOCH 420.


BIOCH 565 - Methods in Molecular Biophysics

Survey of biophysical methods used in the characterization and structural determination of biological macromolecules, from ensemble measurements to single-molecule detection. Topics include mass spectrometry, optical spectroscopy, light microscopy, X-ray and neutron diffraction, electron microscopy, molecular dynamics and nuclear magnetic resonance. Emphasis is on using techniques in evaluating structure-function relationships through the discussion of representative macromolecular systems. Lectures are the same as for BIOCH 465, but with additional assignments and evaluation appropriate to graduate studies. This course cannot be taken for credit if credit has already been obtained in BIOCH 460 or 465.


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