























































Study with the several resources on Docsity
Earn points by helping other students or get them with a premium plan
Prepare for your exams
Study with the several resources on Docsity
Earn points to download
Earn points by helping other students or get them with a premium plan
Community
Ask the community for help and clear up your study doubts
Discover the best universities in your country according to Docsity users
Free resources
Download our free guides on studying techniques, anxiety management strategies, and thesis advice from Docsity tutors
Biochem 301-Exam 1 ACTUAL EXAM WITH QUESTIONS AND 100% CORRECT VERIFIED ANSWERS/ Biochem 301-Exam LATEST 2025-2026 (BRAND NEW!!)
Typology: Exams
1 / 63
This page cannot be seen from the preview
Don't miss anything!
Ionic bond direct interaction between positive and negative ions covalent bond A chemical bond that involves sharing a pair of electrons between atoms in a molecule Electronegativity measure of how strongly atoms attract bonding electrons to themselves molecular weight ratio of the average mass of one molecule of an element or compound to one twelfth of the mass of an atom of carbon-12 (remember that this is a dimensionless quantity) macromolecule a molecule that contains a very large number of atoms. Examples would be proteins, nucleic acids, and carbohydrates. polymer
a macromolecule assembled with covalent linkages between smaller repeating units (Proteins, from amino acids, polysaccharides from carbohydrates, nucleic acids from nucleotides) hydrophobic
Amide sulfhydryl group do Co2 and H2O molecules have the same 3D shape? No because of the distribution of lone pairs of electrons and the hybridization of carbon and oxygen meaning of electronegativity chemical property that describes the tendency for an atom to attract a pair of electrons towards itself how does EN affect the distribution of electrons in a covalent bond between O and H? O = more EN than H
Delta G equation delta G = delta H - T * delta S what does H stand for H = enthalpy (bonding energy); measured in heat units (joule or calories) what does a negative delta H mean? heat is released > exothermic what does a positive delta H mean? heat is consumed > endothermic process what does S stand for? entropy (randomness)
meaning of positive delta G non-spontaneous endergonic (energy-absorbing) meaning of delta G = 0 equilibrium delta G must be (blank) for a reaction to proceed spontaneously negative what else factors into if a reaction will actually proceed (besides having a negative delta G) depends on kinetics and whether there is a pathway by which the reaction might proceed Calculate pH for [H+] = 0.05 M ph = log10 (0.05) = - 1. Calculate pH for [H+] = 0.0001 M
What is the numerical value of "physiological" pH?
Why is the physiological pH nearly constant from cell to cell? because of the biological buffers (phosphate for example) that serve to maintain that pH. what plays an important role in the buffering? why are they necessary proteins; necessary to maintain the max oxygen transfer to hemoglobin
aspirin is absorbed in the stomach where the pH of gastric juice is 1 or in the small intestine where the pH is about 6.
adopts a wide range of random conformations and does not exhibit biological activity or function metalloprotein
True of False? Because of the double bond nature of the peptide bond, the polypeptide backbone is free to rotate at random, providing flexibility to the protein. False; NOT free to rotate, REDUCED flexibility True of False? It is necessary to break peptide bonds in order to denature a protein False; it is NOT necessary True of False? Hydrophobic amino acid residues are usually found on the outside surface inside of globular proteins that is exposed to water molecules. False; found on the INSIDE True of False? Upon cooking, the change in color from clear to solid white is the result of irreversible denaturation of proteins, including albumin, in egg white. True True of False?
Because hydrogen bonds are so weak, but they contribute little to the secondary or tertiary structure of polypeptides. False; they contribute critically to the 2/3 degree structure because there are so many True of False? Many proteins that have a structural or protective role for an organism are insoluble in water and have a fibrous shape. True Botulinus toxin is one of the most poisonous substances known. It is sometimes produced by the bacterium Clostridium botulinum when food is improperly canned and can be fatal when consumed. However, contaminated food can be detoxified by boiling for 20 minutes or more. From this information, is the toxin an inorganic compound, a protein, or a nucleic acid?
primary structure of Protein the amino acid sequence of the polypeptide chain secondary structure of Protein alpha helix and beta pleated sheet alpha helix A spiral shape constituting one form of the secondary structure of proteins, arising from a specific hydrogen-bonding structure. beta pleated sheet One form of the secondary structure of proteins in which the polypeptide chain folds back and forth, or where two regions of the chain lie parallel to each other and are held together by hydrogen bonds. Tertiary structure of protein Defined by the hydrophilic and hydrophobic interactions between R groups of amino acid chains. Forms larger 3D shape quaternary protein structure association between two or more polypeptide chains within one protein
Bohr effect a decrease in the amount of oxygen associated with hemoglobin and other respiratory compounds in response to a lowered blood pH resulting from an increased concentration of carbon dioxide in the blood. write out the equation for the formation of bicarbonate ion from the reaction between water and CO that is catalyzed by carbonic anhydrase CO2 +H2O ⇌ H2CO3 ⇌ H+ + HCO3- General features of the Bohr Effect: metabolizing tissue vs. lungs