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Principles of Life
Principles of Life

... After the tertiary structures of proteins were first shown to be highly specific, the question arose as to how the order of amino acids determined the three-dimensional structure. The second protein whose structure was determined was ribonuclease A, an enzyme from cows that was readily available fro ...
Group : Nanochemical Biology Project : Tyrosine cross
Group : Nanochemical Biology Project : Tyrosine cross

... into tyrosine radicals, which then cross-react with other amino acid residues (mostly tyrosine). A major drawback of the HRP is its high reactivity, leading to dirty products that are very difficult to purify; this drawback is circumvented using a HRP mimicking DNAzyme. Furthermore, the HRP enzyme i ...
HMG B domain
HMG B domain

... conformation of DNA A single AT-hook preferentially binds to stretches of 4-6 bp of AT-rich sequence, and partially neutralizes the negatively charged backbone phosphates on only one face of the DNA helix.  The number and spacing of AT-rich binding sites in DNA influences the conformation of bound ...
Transduction Kit for Peptides and Proteins
Transduction Kit for Peptides and Proteins

... of the transduction cocktail contain a nuclear localization sequence and are therefore able to transport a cargo into the nucleus. The Kit further contains compounds for increasing rate and efficiency of transduction. DMSO enhances the permeability of cell membranes. BSA protects to some degree the ...
Definition (956.3 KB)
Definition (956.3 KB)

... The term protein quality refers to the ratio of essential amino acids (eaa) in a protein in comparison with the ratio required by the body. A high quality protein contains eaa in a ratio that matches human requirements. A protein which is lacking or low in one or more eaa is termed a low quality pro ...
Membrane Structure and Function - AP-Science-Experience-JMHS
Membrane Structure and Function - AP-Science-Experience-JMHS

... flaccid: plasmolysis: ...
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Use of Cell-Free Protein Production Platform for X
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... than the previous work and had a different space group. The structure obtained from cell-free translation (PDB 3KDF, see below) had a better resolution of 2 Å. An important feature of this work was that the open nature of cell-free translation was successfully exploited to assemble target solved by ...
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Protein Electrophoresis
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lecture 5
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... Protein Folding •  Proteins fold to the lowest-energy fold in the microsecond to second time scales. How can they find the right fold so fast? •  It is mathematically impossible for protein folding to occur by randomly trying every conformation until the lowest-energy one is found (Levinthal’s para ...
The biomolecules of terrestrial life
The biomolecules of terrestrial life

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Aromatic Amino Acids
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Ion Exchange Chromatography
Ion Exchange Chromatography

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... (A) Structural features of Tt H-NOX. (B) Heme binding pocket.H-NOX proteins also exhibit remarkable diatomic ligand selectivity despite a similar protein fold. For example, the H-NOX domain from Vibrio cholera (a facultative aerobe) binds NO in a high spin 5-coordinate complex and excludes oxygen, w ...
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Steven Bhutra - Proteomics of Alzheimer's Disease
Steven Bhutra - Proteomics of Alzheimer's Disease

... identify accurately anything under 3.5 on the pH scale, and due to posttranslational changes, many proteins can not be tracked back to their original strand. Because of the relatively small sample size and of gel problems, many protein changes in neuronal diseases may exist but have been missed beca ...
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... XXXX: Peptides identified by MALDI-TOF and by Nano LC-MS/MS on CABYV structural protein sequences. Potential N-glycosylation consensus sites are underlined ...
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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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