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pathologic-cplxs+operons - Bioinformatics Research Group at
pathologic-cplxs+operons - Bioinformatics Research Group at

...  Uses E. coli experimentally verified data as a training set.  Compute log likelihood of two genes being WO or TUB pair based on intergenic distance. ...
Expanded protein information at SGD: new pages and proteome browser.
Expanded protein information at SGD: new pages and proteome browser.

... including: Description, which provides a brief synopsis of the function and/or role of the gene product within the cell; Name Description, which contains the expanded form of the standard gene name acronym; and gene product, which describes the specific function of the protein when it is known. Thes ...
chapter 13 section 2 notes
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... The specific amino acids in a polypeptide, and the order in which they are joined, determine the properties of different proteins. The sequence of amino acids influences the shape of the protein, which in turn determines its function. ...
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Major Trends in Biomedical Research

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appendix 1

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... b. Endoplasmic reticulum (ER) occurs in two forms: smooth and rough - know EACH of the following 1. Rough ER functions to compartmentalize the cell, serves as a mechanical support, provides site-specific protein synthesis with membrane-bound ribosomes and plays a role in intracellular transport 2. ...
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... • Free ribosomes synthesize proteins for use primarily within the cell. • Bound ribosomes synthesize proteins primarily for secretion or for use in lysosomes. • The sequence and number of amino acids in the polypeptide is the primary structure. • The secondary structure is the formation of alpha hel ...
View Full PDF - Biochemical Society Transactions
View Full PDF - Biochemical Society Transactions

... from particular biological sources. The chapter on lysosomal enzymes has been almost completely rewritten, and contains extremely useful and comprehensive reviews on all of those enzymes currently considered to be associated with lysosomes. Relevant biochemical information concerning these enzymes, ...
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... • Yeast episomal plasmids (YEps). • Yeast integrating plasmids (YIps) • Yeast artificial chromosomes (YACs) • Yeast episomal plasmids have been used extensively for the production of eitehr intra- or extracellular heterologous proteins. • Typically, vectors function in both E. coli and S. cerevisiae ...
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... Note also that they all also have a side chain (also called an organic group, an R group, or a functional group), and that each amino acid’s side chain is different from the other amino acids’ side chains. Some are larger than others. Some are electrically charged, while others are electrically neut ...
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... The role of -stacking interactions in chemistry • Amyloid fibril formation is basically a process of intermolecular recognition and self-assembly, the -stacking can provide: • 1) an energetic contribution that stems from the stacking itself; such a contribution can thermodynamically drive the self- ...
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... 2. Use any secondary structure prediction method to predict the secondary structure of 1O8V and compare it to the solved structure. NOTICE! The secondary structure definition in PDB is given in a 7 letter code instead of 3 letter code (H, E, C). For comparison purposes consider: G H and I as H; E as ...
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Diversity in biological molecules

... the amino acid sequence of trypsin from a range of different animal species. The first message here is that the software has been able to align the trypsin sequences even though some of the organisms diverged hundreds of millions of years ago. A second key point is that some parts of the sequences a ...
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Protein adsorption



Adsorption (not to be mistaken for absorption) is the accumulation and adhesion of molecules, atoms, ions, or larger particles to a surface, but without surface penetration occurring. The adsorption of larger biomolecules such as proteins is of high physiological relevance, and as such they adsorb with different mechanisms than their molecular or atomic analogs. Some of the major driving forces behind protein adsorption include: surface energy, intermolecular forces, hydrophobicity, and ionic or electrostatic interaction. By knowing how these factors affect protein adsorption, they can then be manipulated by machining, alloying, and other engineering techniques to select for the most optimal performance in biomedical or physiological applications.
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