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... -tertiary structure – folded shape of the polypeptide chain -quaternary structure – interactions between multiple polypeptide subunits Protein folding is aided by chaperone proteins. ...
Structure-function study of the C-terminal tail of Thioredoxin Reductase
Structure-function study of the C-terminal tail of Thioredoxin Reductase

... Thioredoxin reductase (TR) is an enzyme that functions in maintaining cellular redox homeostasis and protecting the cell from oxidative damage. TR is the only enzyme that reduces the protein thioredoxin, which functions in further reducing proteins and other cellular substrates. This system works as ...
Slide 1
Slide 1

... An OH from the acid group of one amino acid joins to an H from the amino group of the other amino acid. A water molecule is formed, and a C-N bond is formed between the two amino acids. ...
DNA AND PROTEIN SYNTHESIS
DNA AND PROTEIN SYNTHESIS

... (methionine) to the ribosome. • Each tRNA carries one type of amino acid. • The anticodon (three nitrogen bases on tRNA) must complement codon for amino acid to be added to protein chain ...
The Biotechnology Age: Issues and Impacts
The Biotechnology Age: Issues and Impacts

... • 1000’s different enzymes -> unique activities ...
Lecture 4 - Linn-Benton Community College
Lecture 4 - Linn-Benton Community College

... Proteins that carry other molecules from one place to another ...
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... longer needed, damaged or dead organs such as blossoms and leaves are also cast off by a process known as abscission. By doing so, plants conserve energy and prepare for the next step in their life cycle. But how does a plant know when it is the right time to get rid of unnecessary organs? Researche ...
Genetic Controls in Eukaryotes
Genetic Controls in Eukaryotes

... - Roles of transcription factors (enhancers & repressors) o To initiate transcription requires transcription factors. o Bind to promoter (TATA box); RNA Pol II can bind o “General” transcription factors leads to slow transcription. - General = essential to initiation of transcription of all protein ...
CHAPTER 6
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... databases for related genes of interest Alignments between the query sequence and any given database sequence, allowing for mismatches and gaps, indicate their degree of similarity The structure, function, and evolution of a gene may be determined by such comparisons ...
Molecules of Life MBBS Prof. Fridoon
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LC-MRM, a rapid tool for high throughput quantification

... selected protein expression in cells. Despite decades of interest of the scientific community to engineer nucleic acids for therapeutic use, mRNA has only recently been recognized as a revolutionary human therapeutic agent (Thess et al. 2015). mRNA is a carrier of genetic information which recruits ...
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Human Proteome advertising miniposter (PDF)

... viruses. The antibody recognizes a unique part of the foreign target, the antigen. The unique properties of antibodies are used in a wide range of therapeutic and research applications. This poster describes some of the most common techniques. ...
Expediting Purification of Cellular Proteins
Expediting Purification of Cellular Proteins

... from focusing on small numbers of molecules or cellular events to global functional analysis, feeding these results into new approaches for the prevention, diagnosis, and treatment of cancer. Methods that allow researchers to look across a broader angle at cellular processes such as mRNA expression ...
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... Special Features of Protein-Protein Interfaces • Critical for macromolecular recognition • Typically, ca. 500 - 1500 Å2 of surface buried upon complex formation by two globular proteins • Epitopes on protein surface thus may have a “hybrid” character, compatible with both a solvent-exposed (‘free”) ...
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... 1° Primary – the sequence of amino acids in a polypeptide chain. e.g. Met-Val-Leu-Val-Trp-Gly 2° Secondary – polypeptide chain coils into alpha helix and beta pleated sheet due to H bonding. 3° Tertiary – overall shape assumed by each polypeptide chain-Protein 3-D structure determined by interaction ...
Gene Control of Cellular Activities
Gene Control of Cellular Activities

... ƒ Carries information from the nucleus to the cytoplasm and helps in the protein synthesis mechanisms of cell. ...
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Biochemistry

... 1. Bond with many different elements. 2. Forms millions of different, large ...
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... • Proteins can have 4 different structural levels of organization. • Primary Structure: is the sequence of its amino acids. • Secondary Structure: the folding or coiling of a peptide chain. Typically done ...
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BIOL 103 Chapter 1-11 Review

... 1. Animal: effects of nutrients on animals 2. Cell culture: effects of nutrients on cells 3. Epidemiological: study of disease/death rates in population to identify factors that may be related to cause of disease • Correlation is not always causation ...
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... andior histidine. For these, conjugation labelling methods are necessary. Alternative active4 ester derivatives have been described since; presumably these would have been developed independently under the pressure of a need for such methods. “Rudinger sadly died in the mid-1970s. Hunter is now reti ...
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2.24 MB - KFUPM Resources v3

...  Key is the flexibility of proteins allowing them to perform many functions in the organism ...
Distinguish between these 3 root types: - mvhs
Distinguish between these 3 root types: - mvhs

... Ribosome– The “workbench” where translation takes place. Catalyzes the formation of __________ bonds between amino acids to form the polypeptide chain. Made of ________ and rRNA. ...
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... • Can be accomplished using 10-100 nm Au or Ag particles or films ...
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Lecture 3

... Folds in polypeptide that form a more stable structure, often involving hydrogen bonding between R groups There are two types of secondary structure: Helical structure called an alpha helix (α-helix) (region of polypeptide chain coils around itself Pleated sheet (β sheet(: two parts of polypeptide c ...
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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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