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Chapter 5
Chapter 5

... less fluid than unsaturated fatty acids • “Kinks” introduced by the double bonds keep them from packing tightly • Most membranes also contain sterols such as cholesterol, which can either increase or decrease membrane fluidity, depending on the temperature ...
DNA to Protein
DNA to Protein

... but many genes code for more than one product … ...
Chapter 5 PowerPoint
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... less fluid than unsaturated fatty acids • “Kinks” introduced by the double bonds keep them from packing tightly • Most membranes also contain sterols such as cholesterol, which can either increase or decrease membrane fluidity, depending on the temperature ...
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... fats (store and transport energy) lipids (e.g. cell membranes) – these have a crucial “amphiphilic/amphiphobic” property due to their structure and that of water. These are important, especially for life today and probably for the first cells (which may have predated proteins or nucleic acids). But ...
Photo Album
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... The first microtubule motor identified in nervous tissue was a kinesin 1, but studies in mammalian genomes identified 3 kinesin 1 genes, including a neuron-specific form (kinesin 1A). Motor domains are well conserved in all kinesin superfamily genes, but tail domains are more variable and only show ...
Mini-Review Roles of Molecular Chaperones in Protein Degradation
Mini-Review Roles of Molecular Chaperones in Protein Degradation

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6_Petrin_prot_DBs_2011
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propy: a tool to generate various modes of

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ULLA Summer School 2005
ULLA Summer School 2005

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Heat Shock Proteins and Neurodegenerative Disorders
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Directed Proteomics Identifies a Plant
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... Conserved between Arabidopsis and Tomato Previously, we reported that AtMPK6, the ortholog of the MAPK activated by elicitors in tomato (Romeis et al., 1999), was activated similarly by microbial elicitors in Arabidopsis (Nühse et al., 2000). In this work, we found that the Phos43 protein was phosph ...
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Vitamin A - Denton ISD
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No Slide Title
No Slide Title

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... a. mRNA enters the ribosome. b. rRNA reads the mRNA strand and assists in the assembly of proteins c. tRNA has a 3 nucleotide anticodon on one end and its corresponding amino acid attached to its other end. It gets the amino acid from the cytosol. d. tRNA carrying the amino acid methionine at one en ...
a more thorough description of current interests.
a more thorough description of current interests.

... combining traditional shape-selective organic ligands with reveresible coordination to side-chain Lewis bases, such as histidine or methionine, we develop inhibitors for “undruggable” interactions that are both potent and specific. We initially reported rhodium-based stabilization of coiled coils (F ...
MSDA tutorial: How to read output Excel files obtained from GO
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... MSDA tutorial: How to read output Excel files obtained from GO ontologies extractions. In the output Excel file you get after GO ontologies extraction, multiple columns will have been added to the initial input Excel file. These columns include general information about genes/proteins, and specific ...
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What is trans-acting factor?

... 3’untranslated region of more stable mRNAs, they, too, become unstable. • Chemical factors, such as hormones, may also affect mRNA stablility. • In the toad Xenopus laevis(非洲爪蟾) , the vitellogenin gene(卵黄生成素) is transcriptionally activated by the steroid hormone estrogen(类固醇激 素 ) . However, in addit ...
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Protein moonlighting



Protein moonlighting (or gene sharing) is a phenomenon by which a protein can perform more than one function. Ancestral moonlighting proteins originally possessed a single function but through evolution, acquired additional functions. Many proteins that moonlight are enzymes; others are receptors, ion channels or chaperones. The most common primary function of moonlighting proteins is enzymatic catalysis, but these enzymes have acquired secondary non-enzymatic roles. Some examples of functions of moonlighting proteins secondary to catalysis include signal transduction, transcriptional regulation, apoptosis, motility, and structural.Protein moonlighting may occur widely in nature. Protein moonlighting through gene sharing differs from the use of a single gene to generate different proteins by alternative RNA splicing, DNA rearrangement, or post-translational processing. It is also different from multifunctionality of the protein, in which the protein has multiple domains, each serving a different function. Protein moonlighting by gene sharing means that a gene may acquire and maintain a second function without gene duplication and without loss of the primary function. Such genes are under two or more entirely different selective constraints.Various techniques have been used to reveal moonlighting functions in proteins. The detection of a protein in unexpected locations within cells, cell types, or tissues may suggest that a protein has a moonlighting function. Furthermore, sequence or structure homology of a protein may be used to infer both primary function as well as secondary moonlighting functions of a protein.The most well-studied examples of gene sharing are crystallins. These proteins, when expressed at low levels in many tissues function as enzymes, but when expressed at high levels in eye tissue, become densely packed and thus form lenses. While the recognition of gene sharing is relatively recent—the term was coined in 1988, after crystallins in chickens and ducks were found to be identical to separately identified enzymes—recent studies have found many examples throughout the living world. Joram Piatigorsky has suggested that many or all proteins exhibit gene sharing to some extent, and that gene sharing is a key aspect of molecular evolution. The genes encoding crystallins must maintain sequences for catalytic function and transparency maintenance function.Inappropriate moonlighting is a contributing factor in some genetic diseases, and moonlighting provides a possible mechanism by which bacteria may become resistant to antibiotics.
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