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Highligh in Physics 2005
Highligh in Physics 2005

... The study of phenomena taking place in proteins that can only be described by quantum mechanics is particularly complicated, due to the large size of the system and the lack of symmetries. In these cases, a possible approach is to describe quantum-mechanically only a part of the whole protein, accou ...
Protein Targeting
Protein Targeting

... folded before their export from ER ...
The molecular architecture, macro-organization and functions of the
The molecular architecture, macro-organization and functions of the

... Light-harvesting complex II (LHCII), the major antenna pigment-protein complex of plants and green algae, is the most abundant membrane protein on Earth. The primary function of LHCII is to capture sunlight and transfer the excitation energy to the photochemical reaction centers – with up to nearly ...
November 19, 2012 3:00 PM Livermore Center 101  Isaac C. Sanchez
November 19, 2012 3:00 PM Livermore Center 101 Isaac C. Sanchez

... combination of molecular dynamics (MD) and Monte Carlo methods for 6 thermally rearranged (TR) polyimides and their precursors. Diffusion, solubility, and permeation of gases in TR polymers and their precursors were simulated at 308 K, with results that agree with experimental data. A similar method ...
Center for Structural Biology
Center for Structural Biology

... *To characterize properties, separate the protein from all other cell contents* ...
View video content as a PDF
View video content as a PDF

... The Final 3-Dimensional Shape of the Protein Once the secondary structures of a protein have been folded, the model must be given the correct overall shape. When doing this it is very useful to refer back to the online visualization environment. This display can be edited to match what the final phy ...
chapter_6_-_plus_ch_review
chapter_6_-_plus_ch_review

... include carboxyl group, amine group and R group. 3. The bonds between the protein’s building blocks have a specific name – what is it? 4. A simple chain of these building blocks is not a completely functional protein. What has to happen to the chain to make a functional protein? 5. What does the ter ...
Endosymbiosis and Evidence for Endosymbiosis
Endosymbiosis and Evidence for Endosymbiosis

... • Example of a disorder caused by a mutation in a gene that codes for the cell membrane. • CFTR (protein channel) sheets line sweat glands, airways, sinuses, ducts in the digestion and reproduction system. • Allows mucus to slide freely on these linings • Mutation= no hypertonic condition is establi ...
Gene Section AKAP9 (A kinase (PRKA) anchor protein (yotiao) 9)
Gene Section AKAP9 (A kinase (PRKA) anchor protein (yotiao) 9)

... Note: Breakpoint in AKAP9-BRAF fusion is located within intron 8 of the gene. In this fusion, exons 1-8 of AKAP9 are fused with last 10 exons 9-18 of BRAF. In the fusion, AKAP9 lacks the centrosome binding domain and, as a result, the AKAP9-BRAF protein looses its cytoplasmic compartmentalization an ...
Chapter 6 Crossword Puzzle
Chapter 6 Crossword Puzzle

... disassembled into amino acids Increased dietary protein intake can lead to increased excretion of the mineral _____. Amino acids can be used to make glucose if insufficient dietary _____ are consumed. What the body uses to assemble its own proteins Proteins that act to defend the body from disease P ...
control biological machines
control biological machines

... Circuit design Copper wiring width 0.2m ...
Combinatorial docking approach for structure prediction of large
Combinatorial docking approach for structure prediction of large

... Similar structures are clustered together to avoid redundancy and a final list is made. An important note to make is that the program cannot predict whether proteins will combine and form an assembly, but rather knowing that they do form some sort of complex can determine its native conformation. Th ...
Introduction to Protein Science Architecture, Function
Introduction to Protein Science Architecture, Function

... Simplest change to a protein is the substitution of a single amino acid Then, what is the effect on the protein structure and function? ...
blumberg-lab.bio.uci.edu
blumberg-lab.bio.uci.edu

... comparing with an independent yeast two-hybrid project that used different strategies ...
Metal Regulation and Signalling - Zn Proteins
Metal Regulation and Signalling - Zn Proteins

... Structural Zn proteins have different functions, but all create interfaces for macromolecular interactions: protein-protein, protein-DNA, protein-RNA, protein-polysaccharides. No Zn binding motifs found in the e. coli genome, in contrast to an abundance of motifs in eukaryotic cells. Speculation tha ...
Übung: Monte Carlo, Molecular Dynamics
Übung: Monte Carlo, Molecular Dynamics

... water spherical (like a football / billiards ball) or some different shape ? 5. Exam example question with many possible answers: Describe a low-resolution protein model which can ...
Proteins - CasimiroSBI4U
Proteins - CasimiroSBI4U

... peptide bonds, arranged in a specific linear sequence.  Peptide bond = covalent bond formed by condensation reaction that links carboxyl group of one amino acid to amino group of another. ...
BB 450/500 Lecture 5 Highlights
BB 450/500 Lecture 5 Highlights

... Myoglobin contains a heme group that contains iron. Heme is a 'prosthetic group', which refers to a non-amino acid containing group that binds to a protein and augments its function. 8. Amino acid residues in myoglobin are arranged such that hydrophilic (and what your book calls ionic) amino acids a ...
No Slide Title
No Slide Title

... • protein concentration extrapolated from standard curve • sample not recoverable ...
FROM TRAIT TO PROTEIN - CLASSROOM
FROM TRAIT TO PROTEIN - CLASSROOM

... Part I Proteins are large, complex macromolecules that play critical roles in the body. Proteins are made up of hundreds or thousands of smaller units called amino acids, which are attached to one another in long chains. There are 20 different types of amino acids that can be combined to make a prot ...
Macromolecules of life: Structure-function and Bioinformatics 356
Macromolecules of life: Structure-function and Bioinformatics 356

... Faculty of Natural and Agricultural Sciences ...
Protein Engineering
Protein Engineering

... •Increase proteins resistance to proteases (purification) •Signal sequences - secretion •rare codon changes ...
Estimation of the protein secondary structure in aqueous solutions
Estimation of the protein secondary structure in aqueous solutions

... IR absorption spectra. N.M.Romanov The secondary structure of proteins is very important for their proper functioning. The investigation of the secondary structure gives us an insight into the mechanisms of protein functioning in the living cell. IR absorption spectroscopy provides the opportunity t ...
John Torri Basic Nutrition Special Topic: Protein November 13 2014
John Torri Basic Nutrition Special Topic: Protein November 13 2014

... every day. Amino acids are the building blocks for protein. There are two types of amino acids, essential, and non-essential. Essential amino acids are those that are “essential” in the diet. In other words, our bodies cannot create them through our own metabolism. The main essential amino acids are ...
Biochemistry- Ch 11. Carbohydrates
Biochemistry- Ch 11. Carbohydrates

... cell-surface glycoproteins. The viral protein that binds to these sugars is called hemagglutinin. ...
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Bimolecular fluorescence complementation



Bimolecular fluorescence complementation (also known as BiFC) is a technology typically used to validate protein interactions. It is based on the association of fluorescent protein fragments that are attached to components of the same macromolecular complex. Proteins that are postulated to interact are fused to unfolded complementary fragments of a fluorescent reporter protein and expressed in live cells. Interaction of these proteins will bring the fluorescent fragments within proximity, allowing the reporter protein to reform in its native three-dimensional structure and emit its fluorescent signal. This fluorescent signal can be detected and located within the cell using an inverted fluorescence microscope that allows imaging of fluorescence in cells. In addition, the intensity of the fluorescence emitted is proportional to the strength of the interaction, with stronger levels of fluorescence indicating close or direct interactions and lower fluorescence levels suggesting interaction within a complex. Therefore, through the visualisation and analysis of the intensity and distribution of fluorescence in these cells, one can identify both the location and interaction partners of proteins of interest.
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