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Western University
Biology 1001A
Felix Lee

Lecture 1/2 Evolution principles and processes pages 370-372 Evolution does not correlate to complexity. Criteria (bases of) measuring complexity • Genome size of the organism include (number of genes) • Gene number (number of copies of genes) • Number of parts in an organism (Segments, organs, tissues, and etc.) • Number of cell types (variations of types of cells) • Increased compartmentalization (specialization, or specific functions) • Number of interactions of genes (interactions to form parts) • Number of interactions between parts (increased functions) The most commonly used are number of cell types and increased in size of organism. They are factors that reflect life style evolution in the context of complexity. As an organism grows from zygote, the number of cell types varies between one organism to another. The organism with the most variation in the cell types are considered as complex. Evolution of size appears to favor smaller sizes than larger. Between the same size organisms, complexity difference between them is determined by lifestyles. How one reacts to this while the other does another reflects which organism is benefiting more and more efficient. Exploring the diversity of life Chapter 1.1 Light is an essential component of life. It directly and indirectly provides energy to sustain life in all living organisms. Light is used for energy as well as to use it to gather information around the organism. An organism that requires light as source of both energy and information is the common alga Chlamydomonas reinhardtii. It gathers energy through photosynthesis and gathers information to move towards the area with most intensity. Light travels to earth through space from the sun as electromagnetic radiation. “Light” is a portion of the electromagnetic spectrum that human beings can see without any visual aid. (400- 700nm) Light does not have mass but rather is a wave that travels through space as energy known as photons. It is a wave of photons. (*key fact: lower the wavelength greater the energy of photon/ vice versa) Light can interact with matter to cause change despite the fact it has no mass. Photon that interacts with an object will either bounce off, go through, or and be absorbed by the object. The absorption of photon raises the energy of the election of the organism (if photon has energy great enough to overcome orbit energy difference of election). The excitement of election; is the cause of change in object by the interaction of light. Pigments are exceptionally efficient in absorbing light and exist in various types. The carbon bonds that switch from single to double bonds cause the characteristics of absorbing light. This conjugated system, allows the electron to be delocalized and be allowed to interact with photons of light. Many pigments have different wavelength of light that they absorb; it is because or limitability of possible excited electrons. (Pigment colour is the colour being not absorbed but reflected) Lecture 3 Proteins are polymers (20) of amino acids and are most diverse group of biological macromolecules which varies between each other in both their structure and function. Figure on F-28 purple page shows type of protein and their characteristics. Amino acids: a central carbon that has amino group, N terminal (NH2), and carboxyl group, C terminal ,at (COOH) and (H) the remaining bonding site composes with bonds that define the amino acid represented as R (side chain). They have a pH of 7.2 neutral to the body. When discussed in topic of proteins amino acids are labelled as residue (left amino, right carboxyl). Figure on F-29 purple page shows types of side chains associated with property of amino acid. Polypeptides are covalent bonds that link the amino group and the carboxyl group with peptide bond. The results are peptide bonded amino acids and water (dehydration reaction). Primary structure (of protein) is the polypeptide of amino acids (ONLY peptide bond= not functional). Secondary structure is twists and turns due to BOTH the alpha helix and beta sheet (hydrogen bond between Amino/Carboxyl groups. Alpha: helixlike, Beta: side by side). Tertiary structure is twists and folding of protein between the R groups (all bonds within the protein; covalent (disulfide bridge), dipole (hydrophobic interactions), london and ionic bonds)- Most flexible, and alterations in change are known as Conformational changes. Quaternary structure is arrangement of polypeptides (multiple proteins bond together). – Cofactors are non-protein chemical compound that is required to bind to a protein for proper function. DOMAINS of protein – often proteins are divided by sections known as domains connected by random coils created by hydrogen bonds. The divided domains work separately from each other. Ie. One domain builds while the other corrects the mistakes along the process. Chaperone proteins- they are proteins that enwraps the new synthesized protein in order to fold them in proper tertiary structure. LECTURE 4 Enzymes allow chemical reactions to occur faster (10 ~10 ) without raising the temperature or pressure. Energy can only
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