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Week 2 of NE 102 Notes

by: Mathu Karthikeyan

Week 2 of NE 102 Notes NE 102

Marketplace > Boston University > Neuroscience > NE 102 > Week 2 of NE 102 Notes
Mathu Karthikeyan

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These note cover lectures from the second week of school.
Introduction to Cellular and Molecular Biology
Class Notes
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This 3 page Class Notes was uploaded by Mathu Karthikeyan on Saturday January 30, 2016. The Class Notes belongs to NE 102 at Boston University taught by Pastorino in Spring 2016. Since its upload, it has received 39 views. For similar materials see Introduction to Cellular and Molecular Biology in Neuroscience at Boston University.

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Date Created: 01/30/16
Lecture 4 Monday, January 25, 2016 2:02 PM • Protein Structure ○ Primary structure: amino acid sequence ○ Secondary structure: alpha-helix and beta-pleated sheets ○ Tertiary structure: overall shape of the protein; for example globular, fibrous, sheet -like ○ Quaternary structure: association with other proteins; for example dimers • Hydrogen bonds ○ Forms exclusively between the carboxyl group of on e residue to the amino group of another residue • Secondary Structure ○ Alpha-helix § Forms when a sequence of amino acids fold to form the shape of a spiral staircase § Because of their structure, al-helix domains can distribute within membranes ○ Beta-sheet § Hydrogen bonds are made between carboxyl (negative) groups one amino acid to the amino group of another amino acid (positive) § Alignments □ Polypeptide chains lying in a certain direction ® Antiparallel ® Parallel □ This makes the beta sheet a very rigid structure • Disulfide Bonds ○ Covalent ○ Cross-link protein chains ○ Reinforce conformation, stabilize proteins, link protein chains ○ Are formed in the ER ○ Founded in secreted proteins • Folding ○ The conformation of a protein influences the protein's structure ○ Shape=function ○ Thermodynamics § The folded state represents the lowest free energy state for that ○ Founded in secreted proteins • Folding ○ The conformation of a protein influences the protein's structure ○ Shape=function ○ Thermodynamics § The folded state represents the lowest free energy state for that specific protein § Free energy: the number of possible of conformations --> so at the protein's primary structure it has the most possible conformation because each amino acid is open to bond with other amino acids § Folding lowers the free energy because it reduces the number of possible conformations § Low free energy means more stability ○ Chaperones § Help with protein folding because proteins can not fold by themselves § If something wrong occurs --> misfol-->oligomer-->fibrils--> amorphous aggregate § Proper folding happens because of intramolecular forces but when misfolding occurs it is because of intermolecular forces • Proteins aggregate and amyloid/insoluble fibrils ○ Diseased primary structure of amino acid chains ○ Then it goes the modification and secondary structures are formed but they are misfolded and have an abnormal conformation ○ Then they go through cleavage/proteolysis or other modification and casue globular intermediates, protofibrils, fiber for misfolded tertiary structures Lecture 5 Friday, January 29, 2012:09 PM • DNA Backbone ○ Nucleotides § Nitrogenous base § Deoxyribose § Phosphate ○ How they Bind § The hydroxyl 3' binds to the phosphate § The side with an unattached phosphate is 5' and the one with an unattached sugar is 3' • DNA Organization in Chromosomes ○ Bacteria have circular chromosomes ○ In eukaryotic cells DNA is organized in long linear, threads ○ DNA molecules are packed in chromosomes ○ In general, eukaryotic cells contain two sets od chromosomes ○ The bands are the concentration of A,T,C,G in the genes ○ Can be colored based on their chemical components=their base make-up • Histones ○ 4 Types § Histone H24 § Histone H2B § Histone H3 § Histone H4 ○ Serves as a core for the DNA to wrap around ○ The histones tails control how tightly the DNA can attach to the bead and how tightly they can stay wrapped ○ Possible Modifications to Histone Tails


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