Intro to Anatomy, Physiology, and Chemical Organization

Practice flashcards covering introductory anatomy and physiology principles, homeostasis, feedback loops, chemical bonding, reactions, pH, and organic macromolecules.

What is the distinction between anatomy and physiology?

Anatomy is the study of structure and form, whereas physiology is the study of body function.

How do anabolism and catabolism differ within body metabolism?

Anabolism is a synthesis reaction ($A + B \rightarrow AB$) that builds molecules, while catabolism is a breakdown reaction ($AB \rightarrow A + B$).

How is homeostasis defined in Chapter 1?

Homeostasis is the continuous physiological process that enables the body to maintain its structure, function, and a stable internal condition.

What are the six levels of structural organization from simplest to most complex?

Chemical/molecular level, cellular level, tissue level, organ level, organ system level, and organism level.

What are the two mechanisms of homeostatic regulation?

Autoregulation (local adjustments by cells, tissues, or organs in response to environmental changes) and Extrinsic Regulation (activities controlled by the nervous system or endocrine system).

How do the nervous system and endocrine system differ when acting as control centers?

The nervous system provides a rapid, short-term response using electrical signals, whereas the endocrine system provides long-term responses over days or weeks using hormones as chemical messengers.

What are the three essential components of a homeostatic mechanism?

1. Receptors (detect stimuli/changes)
2. Control center (receives input and pushes out a command)
3. Effector (responds to the control center to oppose or enhance the stimulus)

What is the body's standard temperature set point in thermoregulation?

$98.6\,^{\circ}\text{F}$ or $37\,^{\circ}\text{C}$.

How do negative feedback and positive feedback differ in body regulation?

Negative feedback maintains dynamic equilibrium by causing fluctuations around a set point, whereas positive feedback amplifies or enhances changes to produce extreme responses.

What are two examples of positive feedback loops provided in the lecture?

Blood clotting and labor.

How are electrons distributed in the valence shells of a Carbon atom ($\text{C} = 6$)?

Carbon has $2\,e^-$ in its first shell and $4\,e^-$ in its remaining valence shell.

What is an isotope?

Isotopes are atoms of the same element that contain different numbers of neutrons (such as Carbon-12, Carbon-13, and Carbon-14).

How does ionic bonding occur to form a salt like $\text{NaCl}$?

Atoms gain or lose electrons to form charged ions; a cation ($\text{Na}^+$) loses an electron and an anion ($\text{Cl}^-$) gains an electron, attracting each other ($\text{Na}^+ + \text{Cl}^- \rightarrow \text{NaCl}$).

What is the difference between nonpolar and polar covalent bonds?

Nonpolar covalent bonds share electrons equally with no change in charge, while polar covalent bonds share electrons unequally, creating areas with partial negative charges due to higher electronegativity (e.g., $\text{H}_2\text{O}$).

How many hydrogen bonds can a single $\text{H}_2\text{O}$ molecule form?

A single $\text{H}_2\text{O}$ molecule can form 4 hydrogen bonds.

How do dehydration synthesis and hydrolysis reactions differ?

Dehydration synthesis ($AH + BOH \rightarrow AB + \text{H}_2\text{O}$) produces water, forms bonds, and is an anabolic process using energy; Hydrolysis ($AB + \text{H}_2\text{O} \rightarrow AH + BOH$) uses water to break bonds and is a catabolic process releasing energy.

What role do enzymes play in chemical reactions?

Enzymes act as biological catalysts that speed up chemical reactions by lowering the activation energy required for the reaction to occur.

How do exergonic and endergonic reactions differ regarding energy?

Exergonic reactions release energy (catabolic), while endergonic reactions require energy (anabolic).

How do electrolytes and nonelectrolytes behave differently in water?

Electrolytes (salts, acids, bases like $\text{NaCl}$) dissociate into ions ($\text{Na}^+$, $\text{Cl}^-$) and conduct an electric current, whereas nonelectrolytes (like glucose, $\text{C}_6\text{H}_{12}\text{O}_6$) dissolve intact due to a hydration shell.

What does it mean for a molecule to be amphipathic?

An amphipathic molecule has both polar (hydrophilic) and nonpolar (hydrophobic) regions, such as phospholipids in the cell membrane.

What is the normal pH range of blood, and how do buffers help maintain it?

The normal pH of blood is $7.35$ to $7.45$; buffers stabilize pH by binding or releasing $\text{H}^+$ ions (e.g., bicarbonate accepts $\text{H}^+$ and carbonic acid releases $\text{H}^+$).

What are the four main functional groups found in organic macromolecules?

Hydroxyl group ($\text{-OH}$), Carboxyl group ($\text{-COOH}$, acts as an acid), Amine group ($\text{-NH}_2$, acts as a base), and Phosphate group ($\text{-PO}_4^{3-}$, stores energy).

What are glycogenesis, glycogenolysis, and gluconeogenesis?

Glycogenesis is the creation of glycogen from glucose; glycogenolysis is the breakdown of glycogen; gluconeogenesis is the breakdown of non-carbohydrate sources (fats, proteins) to convert into energy.

What are the three categories of lipids and their main functions?

1. Triglycerides (glycerol + 3 fatty acids; long-term energy storage, cushioning, insulation)
2. Phospholipids (amphipathic framework for plasma membranes)
3. Steroids (carbon ring structures like hormones and cholesterol)

What three structural components make up an amino acid monomer?

An amine group ($\text{-NH}_2$), a carboxyl group ($\text{-COOH}$), and an R group that distinguishes the specific amino acid.

What characterizes the four levels of protein structure?

Primary (linear chain of amino acids held by peptide bonds), Secondary (folding into alpha helices or beta sheets via H-bonds), Tertiary (3D coiling/folding due to R group interactions), and Quaternary (interaction of 2 or more protein chains).

What causes denaturation of a protein, and what is the outcome?

Excessive heat, extreme pH, or chemicals cause denaturation, leading to a loss of protein shape and subsequent loss of function.