Principles of Physical Biochemistry Principles of Physical Biochemistry Second Edition Kensal E. van Holde Professor. Principles of Physical Biochemistry (van Holde, Kersal E.; Johnson, W. Curtis; Ho, P. Shing). Article (PDF Download full-text PDF. Chemical. Principles of physical biochemistry / Kensal E. van Holde, W. Curtis .. Applications of the Chemical Potential to Physical Equilibria.
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The Second Edition of Principles of Physical Biochemistry provides the most current look at Get your Kindle here, or download a FREE Kindle Reading App. . that we might be trying to probe using the approaches discussed in van Holde. Principles of Physical. Biochemistry. Second Edition. Kensal E. van Holde. Professor Emeritus of Biochemistry and Biophysics. Department of Biochemistry and. Principles of Physical Biochemistry, 2nd Edition. Kensal E van Holde, Oregon State University, Corvallis. Curtis Johnson, Oregon State University, Corvallis.
Bring your questions. Equations sheet for the upcoming exam is here.
Your graded Homework 2 due on Mar 7, is here. For those who are curious: here is a calculation of the probability to find quantum mechanical H. Do download it click here. Prove the genearal relationships for the commutators which I gave you in class. Specifically, evaluate the commutator [A,BC]. Describe, sketch in your own words. Van Holde 1.
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Biomedical and biophysical research was key to these achievements 8 Introduction-1 Structures of Biological Macromolecules Four main types of Biomacromolecules are found in all living organisms; nucleic acids, amino acids, lipids and carbohydrates.
Conformation: Configuration — Defined by chemical covalent bonds , must break bond to change configuration e. L-amino acid, D-amino acid Conformation — Spatial arrangement e.
Nature 14 A few facts about the human genome Each cell in the body contains the complete genome all DNA. Nucleotides are distinguished by the nucleobases, which can be either of the pyrimidine or purine type. Mutated topoisomerases cause cancer. What is the twist of the DNA? There are hundreds of thousands of different proteins look at protein data bank. Many proteins across organisms are related.
Proteins are uniquely folded peptide chains sometimes one peptide chain, sometimes multiple peptide chains. The monomer unit of a peptide chain protein is an amino acid. There are twenty amino acids, common to all organisms. Proteins have primary 1o , secondary 2o , tertiary 3o , and quaternary 4o structure more in the next slides. E nodule D nodule b-hole a-hole Fibrinogen forms fibrin fibers in a blood clot Six polypeptide chains: 2 Aa a. Each has amino group, carboxyl group, R group and a hydrogen in tetrahedral symmetry.
The polarizability of a medium is defined as its dielectric constant D relative to that of a vacuum. The expressions for the energy of long-range interactions are all inversely related to the dielectric of the medium and are therefore weakened in a highly polarizable medium such as water.
With the dielectric constant, we introduce the environment as a factor in stabilizing the conformation of a macromolecule. How the environment affects the weak interactions is discussed in the next section.
In the process, two additional interactions hydrogen bonds and hydrophobicity are introduced that are important for the structure and properties of molecules.
For biopolymers, the relevant environment is basically the solvent within the cell.
Indeed, a large majority of studies on the properties of biological macromolecules are measured with the molecule dissolved in dilute aqueous solutions. This, however, does not present a complete picture of the conditions for molecules in a cell. In addition, the cell contains a very large surface of membranes, which presents a very different environment for macromolecules, particularly for proteins that are integral parts of the bilayer of the membranes.
The interface between interacting molecules also represents an important nonaqueous environment. For example, the recognition site of the TATA-binding protein involves an important aromatic interaction between a phenylalanyl residue of the protein and the nucleotide bases of the bound DNA.
In cases where solvent molecules are observed at the molecular interfaces for example, between the protein and its bound DNA , the water often helps to mediate interactions, but is often treated as part of the macromolecule rather than as part of the bulk solvent.
In support of this, a well-defined network of water molecules has been observed to reside in the minor groove of all single-crystal structures of DNA duplex. Results from studies using nuclear magnetic resonance NMR spectroscopy indicate that the waters in this spine do not readily exchange with the bulk solvent and thus can be considered to be an integral part of the molecule.