Exam 1 Review - General Biology & Physics Concepts

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Flashcards covering atomic structure, thermodynamics, chemical bonds, biomolecules, protein structure, and laws of motion from the Exam 1 Review.

Last updated 9:56 PM on 9/17/26
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27 Terms

1
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<p>Neutron Count Calculation in Neutral Atoms</p>

Neutron Count Calculation in Neutral Atoms

Subtract the atomic number (ZZ) from the mass number (AA) using the formula: Neutrons=AZ\text{Neutrons} = A - Z.

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Primary Driving Force Behind Chemical Bond Formation

Atoms interact to achieve maximum stability by acquiring a full outer electron shell, typically following the octet rule.

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<p>Factors Determining Kinetic Energy Magnitude</p>

Factors Determining Kinetic Energy Magnitude

An object's kinetic energy depends directly on its mass and the square of its velocity, expressed as KE=12mv2KE = \frac{1}{2}mv^2.

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Second Law of Thermodynamics and Heat Flow

Thermal energy spontaneously transfers from hotter objects to colder objects, increasing the total entropy of the universe.

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<p>Role of Water in Hydrolysis Reactions</p>

Role of Water in Hydrolysis Reactions

A water molecule (H2O\text{H}_2\text{O}) is consumed to split a covalent bond holding monomers together within a polymer.

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Structural Property Allowing Phospholipids to Form Bilayers

Their amphipathic nature, featuring hydrophilic phosphate heads and hydrophobic fatty acid tails.

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<p>Bohr Model Electron Shell Capacities</p>

Bohr Model Electron Shell Capacities

The innermost energy level holds up to 22 electrons, while the second energy level holds up to 88 electrons.

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<p>Anabolic Role of Dehydration Synthesis</p>

Anabolic Role of Dehydration Synthesis

It joins individual monomers together into larger polymers while producing water as a byproduct.

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<p>Universal Product of Polymerization via Condensation</p>

Universal Product of Polymerization via Condensation

A small molecule, typically water (H2O\text{H}_2\text{O}), is eliminated for each covalent bond established between monomers.

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<p>Functional Groups Involved in Peptide Bond Formation</p>

Functional Groups Involved in Peptide Bond Formation

The carboxyl group (-COOH\text{-COOH}) of one amino acid binds with the amino group (-NH2\text{-NH}_2) of another.

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Distinction Between Atomic Number and Atomic Mass

Atomic number reflects only proton count, whereas atomic mass represents the combined total of protons and neutrons.

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<p>Cause of Partial Charges in Polar Covalent Bonds</p>

Cause of Partial Charges in Polar Covalent Bonds

Unequal sharing of bonding electrons due to a significant difference in electronegativity between the bonded atoms.

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Condition Required for an Atom to Have No Net Electrical Charge

The total number of positively charged nuclear protons must exactly equal the total number of orbiting electrons.

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Newton's Third Law Principle

When one object exerts a force on a second object, the second object exerts an equal force in the opposite direction on the first.

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Concept of Inertia

The inherent tendency of an object to resist changes in its state of motion unless acted upon by a net external force.

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Structural Cause of Diverse Protein Functions

The precise arrangement of distinct amino acid side chains determines a unique 3D3\text{D} folding pattern suited for specific functions.

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Effect of Carbon-Carbon Double Bonds on Lipid Fluidity

Double bonds introduce kinks that prevent hydrocarbon chains from packing tightly, lowering the melting point and keeping oils liquid at room temperature.

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Molecular Cause of High Surface Tension in Water

Cohesive hydrogen bonds formed between adjacent polar water molecules at the liquid surface.

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Molecular Basis of Hydrophilic Dissolution

Polar or charged substances readily form hydrogen bonds or electrostatic interactions with polar water molecules.

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Forces Stabilizing Tertiary Structure

Interactions among amino acid R-groups, including hydrogen bonds, ionic bonds, hydrophobic interactions, and disulfide bridges.

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Consequence of Disrupting Side Chain Interactions

The tertiary level of protein structure destabilizes and unfolds without changing the primary amino acid sequence.

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Driving Force of the Hydrophobic Effect

Water molecules exclude nonpolar molecules to maximize their own cohesive hydrogen bonding, forcing nonpolar groups to aggregate.

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Bonds Responsible for Primary Protein Structure

Strong covalent peptide bonds linking amino acids in a linear sequence.

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Stabilizing Bonds in Secondary Protein Structure

Hydrogen bonds formed between oxygen and hydrogen atoms along the polypeptide backbone, creating α\alpha-helices and β\beta-sheets.

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Requirement for Quaternary Structure Formation

The functional aggregation of two or more separate polypeptide subunits into a multi-unit protein complex.

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Structural Impact of Cis-Double Bonds in Fatty Acid Chains

They create a persistent bend in the hydrocarbon tail, reducing intermolecular packing and maintaining membrane fluidity.

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Thermodynamic Meaning of Entropy Increase

Energy naturally degrades into less organized, highly dispersed thermal forms, increasing system randomness.