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Pegylation - WordPress.com
Pegylation - WordPress.com

... It is a polymer of ethylene oxide, and different lengths of the polymer have different uses. For the purpose of this presentation we will stick to the name PEG, and limit our explanation to how it can be used to extend the half-life (t1 ) ...
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AASK Additional Activities

... 1. Have each student document the native shape of their folded protein with a digital photo. 2. Ask the students to unfold their protein and then re-fold it. 3. Check the refolded protein against the photo of the native structure. ...
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Biology 3 Study Guide – Exam #1
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... the various functional groups and their properties polymers, dehydration synthesis and hydrolysis general roles and structures of carbohydrates mono-, di- and polysaccharides the functions of cellulose, starch and glycogen general roles and structures of lipids fatty acids, triglycerides, phospholip ...
Comparative Biochemistry
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Integral membrane proteins and free electron lasers
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... dramatic success has been achieved with methods that present a more membrane-like local environment. These include, most prominently, the lipidic cubic phase (Landau & Rosenbusch, 1996) and bicelles (Faham & Bowie, 2002). Membrane protein crystals, though often relatively straightforward to obtain, ...
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2013 version with answers.

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... expression organism lysate, since it was found that the 6x-His tag specifically binds (reversibly) to columns containing Ni+2 [1] . The nickel is chelated to the column with nitrilotriacetic acid (NTA), which is similar to EDTA. Since many proteins now have His-tags, and cells can be transfected to ...
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Amino Acids - Chemistry Courses: About

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Amino Acids, Primary and Secondary Structure
Amino Acids, Primary and Secondary Structure

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Intrinsically disordered proteins



An intrinsically disordered protein (IDP) is a protein that lacks a fixed or ordered three-dimensional structure. IDPs cover a spectrum of states from fully unstructured to partially structured and include random coils, (pre-)molten globules, and large multi-domain proteins connected by flexible linkers. They constitute one of the main types of protein (alongside globular, fibrous and membrane proteins).The discovery of IDPs has challenged the traditional protein structure paradigm, that protein function depends on a fixed three-dimensional structure. This dogma has been challenged over the last decades by increasing evidence from various branches of structural biology, suggesting that protein dynamics may be highly relevant for such systems. Despite their lack of stable structure, IDPs are a very large and functionally important class of proteins. In some cases, IDPs can adopt a fixed three-dimensional structure after binding to other macromolecules.
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