Bio 151-000Academic Coordinator -- Dr. Alma FerrierOffice: Room 216 Thomas Hunt Morgan BuildingSee web site or syllabus for TA and Academic

Coordinator contact information.

Primary TA: NAMEOffice Phone #: xxx-xxxxOffice Location: Where LocatedOffice Hours: Days and hoursEmail: email

Secondary TA: NAMEEmail: email

Syllabus

•Course Description

Bio 151 is the 1st semester of a two semester introductory sequence for life science majors. The companion lecture course is Bio 150. This course is designed to prepare students for upper level Biology courses. Bio 151 is mainly consists of experimentation in the areas of biochemistry, cell and molecular biology, genetics, and evolution. Students will perform experiments, analyze results, and submit their observations in the form of lab reports.

•Attendance:

Attendance is required in the laboratory section to which you are assigned. Five points will be deducted for each unexcused absence

Syllabus

•Improper care and storage of microscopes and messes in your workarea will result in a Five-point deduction each time

•Plagiarism and Cheating -- Read the section covering this in the Students Rights and Responsibilities Handbook, University of Kentucky

Syllabus

Homework For Modules: The homework assignments for modules are a series of worksheets,which you are required to complete during the course of the semester. The homework will consist of questions covering material in the course texts. The assignments may be downloaded from the web sitehttp://www.biology.uky.edu/bio150labs/

Homework must be submitted before the beginning of the class periodfor which they are due (see syllabus for the exceptions) and whichyou are officially registered. Late submissions will not be accepted.

Syllabus

1. Required Texts:

1. Biology by Neil Campbell, 5th or 6th edition,Benjamin Cummings Publishing Company or a Current Introductory Biology Book.

  2. Laboratory Manual Bio 151 7th edition by Doris Westerman

Module 1

Chemosynthetic Theory and Introduction to Simple Amino Acids

Chemosynthetic Theory or “Chemical Evolution": is the abiotic (non-living) synthesis of organic molecules.

Organic Molecules are by definition molecules that containthe element carbon. Once thought to come from only livingthings, organic compounds range from simple molecules such as methane CH4 to colossal ones such as proteins with thousands of atoms.

The elements of life which compose these molecules:

CarbonHydrogenOxygenNitrogenPhosphorusSulfur

Oparin-Haldane hypothesis (1920s):

Primitive Earth’s reducing atmosphere favored chemicalreactions that synthesized organic compounds from inorganic precursors present in the early atmosphere and seas.

Miller-Urey (1953) tested this hypothesis by:

Simulating primitive Earth’s atmosphere with H2O, H2, CH4, CH3, CO, CO2, and N2. Then Exposing this atmosphere to sparks (simulating lightning and providing extreme heat).

Observed the formation of organic molecules, includingamino acids. Thereby allowing the formation of proteins

Figure 26.4  Abiotic synthesis of organic molecules in a model system

Amino Acids and Simple Peptides

There are 20 common amino acids which are important in protein formation.

The R group(side chain) is different for each amino acid and is what gives each amino acid is unique characteristic

Of the 20 amino acids, 19 contain asymmetric "-carbons. These 19 amino acids can form isomers. They isomers have been named L and D. The L-form is what is naturally occurring in living systems. The only amino acid that does not have an L and D form is Glycine (It's R-group is a hydrogen atom).

Amino Acids are joined by an amide bond known as the peptide bond. When the bond is formed, H2O is liberated

Unnumbered Figure (page 68) Amino acid structure

Figure 5.15a The 20 amino acids of proteins

Figure 5.15b The 20 amino acids of proteins

Figure 5.15c The 20 amino acids of proteins

Two enantiomers possible for most amino acids

L-form found almost exclusively in naturally occurring proteins

Assigning Amino Acids as either D or L

EXAMPLE:

The amino acid alanine is shown below. Bonded to its alpha carbon atom are:

a carboxyl group (COO-)

an amino group (NH3+)

a methyl group (CH3)(its R group)

a hydrogen atom

Assigning Amino Acids as either D or L

If you orient the molecule so that you look along it from the COO- group to the NH3

+ group, the methyl (R) group can extend

out to the left, forming L-alanine(shown below on the left) or to the right, forming D-alanine (on the right).

Polypeptides (proteins)

The importance of proteins is implied by their name, whichcomes from the greek word proteios meaning “first place”.

Proteins are the most structurally sophisticated molecules known. Each type having a unique three-dimensional shape or conformation.

Polypeptides are formed by the condensation of multiple amino acids forming a polypeptide chain.

Figure 5.16 Making a polypeptide chain

Formation of a Peptide Activity(10 minutes)

Per Group of Two Gather the Following Materials

• three of the stick models that are in the form of a tetrahedron. Each tetrahedron will symbolize one amino acid.

• 3 purple, 3 green, 3 white, and 3 red gumdrops. These will be placed on the model to symbolize the different parts of the amino acids.

• white gumdrops will symbolize the free hydrogen on the alpha carbon of the amino acid

• red gumdrop will symbolize the amino group that is attached to the alpha carbon

• purple will represent the carboxyl group

• green will represent the R group of the amino acid

Formation of a Peptide Activity(5 minutes)

•Amino acids combine and displace water to form a peptide bond between the amino group of one amino acid and the carboxyl group of another amino acid (Condensation)

•At the cellular level, translation is the process by which polypeptide chains are formed. The N-terminus of an amino acid is joined to the C-terminus of the previous amino acid forming a peptide chain.

•Now, join your three amino acids, one at a time to displace one molecule of water, forming a peptide bond between each amino acid.

Now that you have made polypeptide, what type of

characteristics do these chains exhibit that produce unique

properties to their structure and function?

Read Chapters 1-5 in Campbell and be prepared to discuss this

question next class.

Next class, you will perform some computerexercises during class.

You may download these exercises from the websiteat www.biology.uky.edu/bio150labs . Be sure to See if you can down load the assignment as it willbe due next week.

RASMOL

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