Exam 3: Amino Acids and the Primary Structures of Proteins
Exam 1: Introduction to Biochemistry60 Questions
Exam 2: Water80 Questions
Exam 3: Amino Acids and the Primary Structures of Proteins85 Questions
Exam 4: Proteins: Three-Dimensional Structure and Function101 Questions
Exam 5: Properties of Enzymes80 Questions
Exam 6: Mechanisms of Enzymes75 Questions
Exam 7: Coenzymes and Vitamins80 Questions
Exam 8: Carbohydrates77 Questions
Exam 9: Lipids and Membranes85 Questions
Exam 10: Introduction to Metabolism75 Questions
Exam 11: Glycolysis74 Questions
Exam 12: Gluconeogenesis, the Pentose Phosphate Pathway, and Glycogen Metabolism75 Questions
Exam 13: The Citric Acid Cycle75 Questions
Exam 14: Electron Transport and Oxidative Phosphorylation82 Questions
Exam 15: Photosynthesis70 Questions
Exam 16: Lipid Metabolism75 Questions
Exam 17: Amino Acid Metabolism73 Questions
Exam 18: Nucleotide Metabolism65 Questions
Exam 19: Nucleic Acids83 Questions
Exam 20: Dna Replication, Repair, and Recombination76 Questions
Exam 21: Transcription and Rna Processing75 Questions
Exam 22: Protein Synthesis85 Questions
Exam 23: Recombinant Dna Technology73 Questions
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Although the hydroxyl groups in serine and threonine are uncharged, they can react within active sites of some enzymes .
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Even though mass spectrometry has been in use for over a hundred years, it had only limited use with proteins until the 1980ʹs because
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A polypeptide chain may have abrupt changes in direction and restriction in geometry because of the presence of
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Basic amino acids are positive, negative at pH 7 and acidic R group amino acids are positive, negative at pH 7.
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