Enzyme kinetics - Study guides, Class notes & Summaries
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Biochemistry ACS Exam Questions and Answers 2024
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structures and properties of amino acids 
Nonpolar, Aliphatic (Hydrophobic): 
Glycine (Gly, G) 
Alanine (Ala, A) 
Valine (Val, V) 
Leucine (Leu, L) 
Isoleucine (Ile, I) 
Proline (Pro, P) 
 
Aromatic (Hydrophobic): 
Phenylalanine (Phe, F) 
Tyrosine (Tyr, Y) 
Tryptophan (Trp, W) 
 
Polar, Uncharged (Hydrophilic): 
Serine (Ser, S) 
Threonine (Thr, T) 
Cysteine (Cys, C) 
Methionine (Met, M) 
Asparagine (Asn, N) 
Glutamine (Gln, Q) 
 
Positively Charged (Basic, Hydrophilic): 
Lysine (Lys, K) 
Arginin...
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Chemistry for Biology Students (CHEM0010) Notes
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Embark on a comprehensive exploration of Chemistry for Biology Students at UCL. Uncover the dynamics of chemical and enzyme kinetics, ions and chemical forces, delve into the principles of spectroscopy, and explore the intricacies of structure, bonding, self-assembly, and thermodynamics in biological molecules.
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MLT Clinical Chemistry Final Exam Latest Version Graded A
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MLT Clinical Chemistry Final Exam Latest Version Graded A Absolute binding Enzymes that can bind only one substrate and catalyze one reaction exhibit which type of binding specificity? 
Double The rate of an enzymatic reaction will ___________________ for every 10 degrees C temperature increase until the enzyme denatures. 
c. Myocardial infarction All of the following conditions may result in a rise in CKBB levels except. 
a. Child birth 
b Spinal chord injury c. Myocardial infarction 
d. Brain ...
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MLT Clinical Chemistry Final exam 2024 with 100% correct answers
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Absolute binding - correct answer Enzymes that can bind only one substrate and catalyze one reaction exhibit which type of binding specificity? 
 
Double - correct answer The rate of an enzymatic reaction will ___________________ for every 10 degrees C temperature increase until the enzyme denatures. 
 
c. Myocardial infarction - correct answer All of the following conditions may result in a rise in CKBB levels except. 
a. Child birth 
b Spinal chord injury 
c. Myocardial infarction 
d. Br...
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Samenvatting Marks' Basic Medical Biochemistry - Biochemistry (AB_1137)
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Chapters: 1 (l, ll), 2, 3, 4, 5, 6, 7, 8, 9, 10 (l, ll), 19 (l, ll), 20, 22, 23, 24, 25 (l, lll), 26 (l, ll, lll), 27 (l,), 28 (l, ll) 
Thermodynamics, Membrane transport, Chemical potentials, Enzyme kinetics, Metabolism
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BCHM 313 - April Exam 2024 with 100% correct answers
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Spectroscopy Methods correct answers- Fluorescence Microscopy 
 
- super resolution microscopy 
 
- flow cytometry / mass cytometry 
 
Ligand binding can be tested by correct answers- equilibrium dialysis 
 
- Fluorescence (anisotropy) 
 
- FRET 
 
- SPR 
 
Enzyme kinetics can be tested by correct answers- UV-Vis spectroscopy 
 
- Fluorescence 
 
- FRET 
 
Modes of inhibition correct answers 
 
UV-Vis spectroscopy correct answers- light absorption by chromophores 
- measure the amount of l...
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Tri 1 Biochem Past Exams Questions and Answers Already Passed
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Tri 1 Biochem Past Exams Questions 
and Answers Already Passed 
 
What is the role of zinc in enzyme function? 
 Zinc acts as a cofactor, stabilizing the structure of enzymes and aiding in catalysis. 
 
Which type of bond forms between the amino group of one amino acid and the carboxyl group of 
another? 
 
 A peptide bond forms between the amino and carboxyl groups, linking amino acids together. 
 
How do enzymes use the lock-and-key model to explain substrate binding? 
 The lock-and-key model ...
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Biochemistry Study Guide Questions and Answers Rated A+
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Biochemistry Study Guide Questions 
 
and Answers Rated A+ 
 
What unique feature of enzymes allows them to be highly specific for their substrates? 
 The unique three-dimensional shape of an enzyme allows it to fit only specific substrates, 
much like a key in a lock. 
 
How does the structure of glycogen contribute to its function as an energy reserve? 
 Glycogen's branched structure allows for rapid mobilization of glucose when energy is 
needed quickly. 
 
What is the significance of the ...
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Grade 12 Biochemistry Test Review Graded A+
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Grade 12 Biochemistry Test Review 
 
Graded A+ 
 
In which organelle does the majority of ATP production occur during cellular respiration? 
 Mitochondria 
 
What is the significance of the R-group (side chain) in an amino acid? 
 The R-group determines the unique properties and functions of each amino acid. 
 
What happens when a protein denatures? 
 The protein loses its three-dimensional structure and can no longer function properly. 
 
How does a phospholipid's structure make it ideal for...
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MCAT Biochemistry Review | Latest Version | 2024/2025 | Graded A+
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MCAT Biochemistry Review | Latest 
Version | 2024/2025 | Graded A+ 
 
What is the primary function of the enzyme catalase in cells? 
 
Catalase breaks down hydrogen peroxide into water and oxygen, protecting cells from 
oxidative damage. 
 
Explain the role of coenzymes in enzyme-catalyzed reactions. 
 
Coenzymes are organic molecules that assist enzymes by providing essential chemical 
groups or by stabilizing transition states during catalysis. 
 
What is the significance of the Km value in en...
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