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COURSE INFORMATION
Biochemistry 3111K
Biochemistry I
Fall Semester 2012
M W F 10:00 AM – 10:50 AM
E 154
INSTRUCTOR: Dr. Rajnish Singh, Rm E 105
Phone:
Email: [email protected]
Office Hours:
Monday 10-11 am, Wednesday 2-4 pm, Thursday 10-11 am
Friday 10-11 am
COURSE MATERIAL:
Lecture Textbook: Horton, Principles of Biochemistry. 3rd edition. PrenticeHall, Inc., Upper Saddle River, NJ.
The text book has a companion website: www.prenhall.com/horton
COREQUISITE:
PREREQUISITE:
BIOC 3111L (Biochemistry I Laboratory)
CHEM 2512K (Organic Chemistry II)
COURSE DESCRIPTION: Biochemistry deals with the CHEMISTRY of biological
molecules: proteins, nucleic acids, lipids, carbohydrates, and metabolic
intermediates. As you have discovered, chemistry deals with many different
aspects of matter, e.g. structure, physical properties, and chemical
properties,including reaction rates, mechanism, etc. Biochemistry is no
exception. Biochemists apply concepts learned in freshman chemistry and organic
chemistry to biological molecules. The one difference between biological
molecules and those seen in organic chemistry is that biological molecules are
usually much larger and most are in an aqueous environment. Biochemistry at SPSU
(and most universities) is divided into two main parts. The first (BIOC 3111)
focuses mainly on the structure and function of the biomolecules while the second
(BIOC 3112) focuses mainly on the synthesis and degradation of these molecules
for energy purposes.
Student learning outcomes will be:
1. understands thermodynamic laws that govern synthetic and degradative
biochemical reactions which are essential to the working of a living cell.
2. understands and can draw the structures of amino acids, fatty acids,
monosaccharides and nucleotides that make up biomolecules required for the
function of a living cell
3. understands buffer mechanism
and their physiological importance
4. understands how monomers assemble into biomolecules, the chemical forces that
stabilize the structure and consequently the function of biomolecules,
particularly proteins and structure and function of fibrous and globular proteins
5. able to use appropriate software to visualize and manipulate secondary and
tertiary structures of proteins and determine non-covalent interactions important
to function of protein
6. comprehends basic principles of enzyme kinetics and the kinetics of enzyme
inhibition
7. understands mechanisms of digestive enzymes such as serine proteases
8. understands the principles of protein separation techniques and is able to
conduct experiments in amino acid titration, SDS-PAGE, gel filteration, ion
exchange and hydrophobic interaction chromatography
GEORGIA VIEW VISTA
The following items will be posted on vista from time to time.
ALL HANDOUTS
LECTURE POWERPOINT SLIDES
STUDY TOOLS
It is the student’s responsibility to make sure he or she can access webCT/vista.
If you have a problem, contact the instructor IMMEDIATELY.
STRUCTURE VISUALIZATION:
Studying structures of macromolecules requires visualizing these molecules and
being able to manipulate these structures. You will be given exercises that
require you to download and view structure files from the Protein data Bank (PDB)
the website for which is www.pdb.org
There are enumerable software that allow you to visualize macromolecules but in
this course, you will be using either of the following 2 programs:
a. SwissPDBviewer
b. VMD(Visual Molecular Dynamics)
http://www.expasy.org/spdbv
http://www.ks.uiuc.edu/Research/vmd
These can be downloaded for free from the websites listed above.
ATTENDANCE:
Regular lecture attendance is essential for success in this course.
LECTURE PREPARATION:
There is a large volume of material to be learned in this course. Success in
this course will require much study out of class; students should expect to study
a minimum of THREE HOURS out of class for every ONE HOUR of lecture. Preparation
for class should include: reading the upcoming material, studying the previous
material, and working problems related to the previous material.
HOMEWORK PROBLEMS & ASSIGNMENTS:
Unless otherwise announced, students should work all of the problems at the end
of each chapter.
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Homework will be assigned after almost every chapter.
Deadlines for homework assignments will be announced in class. Missing class is
NOT a reasonable excuse for not knowing due dates for assignments.
Late homework assignments will NOT be accepted. 10 points will be DEDUCTED for
assignments submitted ON due date, but later than 10:15 am. If you cannot make it
to class that day, you will scan and email assignment before 10 am.
There will be NO exceptions to rule above. If you happen to be sick, assignment
will be accepted ONLY with a doctor’s note.
EXAMS:
There will be 4 in-class exams. All exams will consist of a variety of questions
which may include multiple choice, essay, fill-in-the blanks or short answer
questions.
The FINAL EXAM will be COMPREHENSIVE.
Breakdown of GRADE:
Homework assignments
Best 3 out of 4 exams
Final exam
15%
45 (at 15% each)
20%
Lab
20%
POP/SURPRISE QUIZZES will be given periodically. 2% of average score on quizzes
will be added to your final score at the end of the semester. NO MAKE UP QUIZZES
WILL BE GIVEN, even if you happen to be sick that day and do not make it to
class.
Grading Scale:
90 – 100%
80 - 89%
70 - 79%
60 - 69%
< 60%
A
B
C
D
F
ACADEMIC INTEGRITY:
Academic honesty as detailed in the Student Handbook is expected. All SPSU
students are required to abide by the honor code that can be found in
http://spsu.edu/honorcode/
SCHEDULE OF IN-CLASS TESTS: You will be informed about a test at least two weeks
prior to the date
Test
Test
test
test
1:
2:
3:
4:
chapters 1 and 2
chapter 3 and 4
chapters 5 and 6
chapter 8,9 and 11
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Students with disabilities who believe that they may need accommodations in this
class or laboratory are encouraged to contact the counselor working with
disabilities at the ATTIC as soon as possible to ensure that such accommodations
are implemented in a timely fashion.
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