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Week 1 of Notes

by: Stephanie Morales

Week 1 of Notes BCM 475 - M001

Stephanie Morales
GPA 3.5
Biochemistry I
M. Braiman, R. Welch

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About this Document

Every week I'll include detailed notes from class and the textbook. As well as a study guide before each exam!
Biochemistry I
M. Braiman, R. Welch
Class Notes
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This 2 page Class Notes was uploaded by Stephanie Morales on Monday September 7, 2015. The Class Notes belongs to BCM 475 - M001 at Syracuse University taught by M. Braiman, R. Welch in Fall 2015. Since its upload, it has received 139 views. For similar materials see Biochemistry I in Biochemistry at Syracuse University.

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Date Created: 09/07/15
Biochemistry October 30th First principle biochem has the tendency to duplicate and then modify Second principle everything is measured according to scale Third principle appearance is deceiving and small changes causes large impacts Biochem is chemistry that takes place in living systems dependent upon molecular interactions Biochem mainly focuses on non covalent bonds instead of covalent bonds Examples of non covalent bonds are electrostatic hydrogen bonds and Van der Waals interaction Electrostatic interaction includes an equation Coulombs law which is EEnergyk332 kcalmol q1q2energy of atoms Ddielectric constantx rdistance between atoms Van der Waals is asymmetry of electronic charge Water is very important in biochem It weakens electrostatic interactions and hydrogen bonding by competing their interactions September 2nd Proteins are based on a infinite number of macromolecules structure that can be generated from limited number of building blocks Proteins can be either rigid or considerably exible Such exibility is critical to their function it is aided by levers hinges and springs L isomers and D isomers are mirror images L configurations are constituents of proteins the hydrogen is away from viewer and it has a counterclockwise configuration Glycine is achiral unique it has two hydrogen s coming out Alanine contains aliphatic side chain which is mainly a methyl group Hydrophobic amino acids are larger and are mainly inside the protein to allow hydrophilic interaction Examples are isoleucine has a second chiral center methioninethioester prolinethe R group is connected to the amino group which makes it rigid Aromatic amino acids can participate in Van der Waals interactions Examples are Tyrosine Tryptophan Phenylaline Polar amino acids have a 39OH group It is hydrophilic and some examples include threoninecontains additional chiral carbon Tyrosine Serine asparagine and glutamine Cystine makes disulfide bonds which helps in oxidation Polar hydrophilic and positive amino acid are Lysine and Arginine which are positive Histidine contain imizidiol group September 4th Serine asparate and aspargine also tend to disrupt alpha helices because their sidechains contain hydrogen bonding donors or acceptors in close proximity of the main chain Proline breaks helices because it lacks an NH group Peptide chains have polarity They are planar because within the peptide bonds there is resonance Resonance structures constrain the atoms to a plane and also affects bond lengths They are either cis or trans but the predominant is trans because it minimizes steric hindrance Xpro any amino acid followed by a proline Can exist in cis and trans because steric hindrance occurs in either forms


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