


































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
1. biochemistry exam study strategies for module 1 2. practice questions for biochemistry module exam 3. biochemistry module exam preparation tips 4. best resources for biochemistry module exam review 5. biochemistry exam time management techniques 6. common mistakes to avoid on biochemistry module exam 7. biochemistry module exam format and structure 8. how to ace biochemistry module exam in one week 9. biochemistry exam sample questions with answers 10. biochemistry module exam grading criteria 11. biochemistry exam calculator requirements 12. biochemistry module exam past papers pdf 13. biochemistry exam cheat sheet for quick review 14. biochemistry module exam online practice tests 15. biochemistry exam essay question examples 16. biochemistry module exam retake policy 17. biochemistry exam multiple choice question strategies 18. biochemistry module exam study group near me 19. biochemistry exam formula sheet allowed 20. biochemistry module exam difficulty level
Typology: Exams
1 / 42
This page cannot be seen from the preview
Don't miss anything!
macromolecule.: True
macromolecules.: False
electrons
Alcohols
bonded to one another.: Kekule' structure
.: Supramolecular complex
functional group.: Alcohol
: All of these were discussed.
all eukaryotes, is called the .: Cytoskele- ton
least two sentences.: The fundamental similarity is that each cell type has a plasma membrane that
separates life from non-life. The plasma membrane acts as a barrier to most molecules but does have proteins that permit select molecules to cross via proteins (transporters). The plasma membrane permits the cell to have a different composition of molecules inside the cell than out and defines a space for life to occur.
molecules? Explain which one (smaller or larger) are preferred and give at least two examples of elements (smaller or larger) common in the biomolecules.: According to the Module, are smaller elements or large elements favored in biological molecules? Explain which one (smaller or larger) are preferred and give at least two examples of elements (smaller or larger) common in the biomolecules.
form strong covalent bonds with a variety of different elements.
chemistry is the study of all other elements, but carbon. Organic chemistry is the study of carbon-based compounds both in living and non-living organisms. There is no need to have separate sub-disciples for organic and inorganic chemistry, but for historical and organizational reasons, the difference exists.
what are two other aspects of living organisms that
10-4); acetic acid (Ka = 1.7 x 10-5); phosphoric acid (Ka = 7.3 x 10-3): Acetic acid, nitrous acid, phosphoric acid
that exists between Br2 molecules in the liquid?: London forces
positive and partial negative charges. If a dipole arrow were added to this structure, which way would the arrow point?: The arrow points from N toward Br
product to glue plastic together.: ”G is (-) and ”H is (-)
capacity
indicated by the brackets [ ].: molarity
nonpolar portion of structure. The four molecules interact in such a way that the nonpolar sections align. This is an example of the .: Hydrophobic effect
how about the strength of a hydrogen bond compared to a dipole-dipole force? Briefly comment on these differences.: The hydrogen bond strength is between 12 and 16 kcal, while the London force is generally less than 1 Kcal. A dipole-dipole bond usually is from 0.5 to 2.0 kcal. Also, hydrogen bonds are the strongest non-covalent force, which is illustrated by these numbers 57. : .12 [x-][H+]
D) entropy E) "+"
hydrophobic effect helps scientists explain how biological molecules form and interact. For instance, when molecules with both a nonpolar and polar regions dissolve in water, the nonpolar regions pack together. The packing of the nonpolar regions minimizes the interaction with water and the polar region interact with water, which in total is called the hydrophobic effect. The driving force behind this effect is the spontaneous drive of water to bind to itself through hydrogen bonds. To maximize the hydrogen bonds, water orders itself around the hydrophobic portion of the nonpolar regions in a cage structure also called a clathrate. In so doing, water can form bonds with itself and also permit the nonpolar regions to be dissolved.
Condensation
a .: Protein
acid, D
numbers of each type of secondary structur one alpha helix and two beta strands (or one beta sheet). Beta turns m but are not required in the answer.
what level of protein organization?: A) Simply it means that hemoglobin has four subunits or four independent polypeptide chains interacting non-covalently. Each protein molecule is composed of two copies each of two different subunits a and b. We say that hemoglobin is a tetramer because it has four polypeptide chains. B) It is describing the quaternary structure, which has two or more independent polypeptide chains that associate with one another to form a quaternary structure.
structure. What is the name of the collections of protein structure? Explain this type of structure.: Motifs occupy a position between secondary and tertiary. Motifs are particularly stable arrangements of secondary
structure, including the connections between them. Motifs are found in a variety of proteins from across all organisms.
Explain in at least two complete sentences.: The "PRSGED" is an example of protein primary structure, which is the order of amino acids in a peptide or protein. Each of the letters (i.e. P, R, ...) represents one of the 20 amino acids as a one-letter abbreviation). The order of amino acids is written from N-terminal to C-terminal. The letters in this peptide stand for Proline, Arginine, Serine, Glycine, Glutamic Acid, and Aspartic Acid.
spot.: The active site is the spot on the enzyme where catalysis takes place. This area is often small when compared to the overall size of the protein. In fact, about 10 amino acids make up the active site.
atom
A) D-ribose and D-galactoseB) ±D- -allose and ²-D-alloseC) D-Ribose and L-fruc- toseD) D-glucose and L-glucoseE) ±D- -idose and ²-L-idose: ±D- -allose and ²-D-al- lose
reaction occurs
A) ±D- -glucoseB) ²-D-glucoseC) GalactoseD) IdoseE) Maltose: ±D- -glucose
.: Glucose
A) ±B) C² ) DD) LE) Both A and C: D
structure in proteins.
A) ±and B² ) D and LC) Anomer and epimerD) Furan and pyranE) Both A and B: A
He runs across several beetles with hard chitin exoskeletons. Would he get nutrition in the form of glucose from eating these beetles? Explain.: The human enzyme cannot break down the bond between the glucose residues in chitin. The bond is a ²1 ’4,but human enzymes only act upon ± 1 ’4S. o, no he should not eat the beetles as food.
different?: An oligosaccharide is a polymer of 2 to 20 monosaccha- rides joined together. A polysaccharide is more than 20 monosaccharides joined together. They are typically linked together by the same1 ’ 4 linkages
practically, and there are usually thousands of monosaccharides in a polysaccharide. In addition, polysaccharides can have branches in the structure, which permits them to form large complexes. In contrast, most oligosaccharides do not have branching.
letter corresponding the correct carbon ("A", "B", etc.)