atomic force microscopy(AFM) and circular dichroism(CD) in protein structure analysis?
460188
AFM collect surface atomic data\nCD collect absorbance which reveal the secondary structure\nCD 2nd structure and low resolution\nAFM higher resolution and study the whole structure
845828
Here you go...\n\nhttp://home.planet.nl/~skok/techniques/laboratory/pka_pkb.html
725118
Please follow the links\nhttp://www.BIO-MEMS.ORG \nhttp://www.BIOINFORMATICS.CC \nhttp://www.BIOTECH-RESEARCH.INFO \nhttp://www.BIOTECH-RESEARCH.NET \nhttp://www.BIOTECHRESEARCH.BIZ
171613
Electrophoresis, x-ray diffraction (x-ray crystallography), chromatography (usually use for plant cell), centrifugation, microscope, and by using fluorescence technology
785808
usually protein with some metallic ions
122666
http://www.seedbiology.de/structure.asp
901348
well let me think...ITS A DOUBLE HELIX!!!!!!!!!!!!\nDOUBLE          DOUBLE               DOUBLE
1092286
alpha-Crystallin is a major lens protein, comprising up to 40% of total lens proteins, where its structural function is to assist in maintaining the proper refractive index in the lens. In addition to its structural role, it has been shown to function in a chaperone-like manner. The chaperone-like function of alpha-crystallin will help prevent the formation of large light-scattering aggregates and possibly cataract. In the lens, alpha-crystallin is a polydisperse molecule consisting of a 3:1 ratio of alpha A to alpha B subunits. In this study, we expressed recombinant alpha A- and alpha B-crystallin in E. coli and compared the polydispersity, structure and aggregation state between each other and native bovine lens alpha-crystallin. Using gel permeation chromatography to assay for polydispersity, we found native alpha-crystallin to be significantly more polydisperse than either recombinant alpha A- or alpha B-crystallin, with alpha B-crystallin having the most homogeneous structure of the three. Reconstructed images of alpha B-crystallin obtained with cryo-electron microscopy support the concept that alpha B-crystallin is an extremely dynamic molecule and demonstrated that it has a hollow interior. Interestingly, we present evidence that native alpha-crystallin is significantly more thermally stable than either alpha A- or alpha B-crystallin alone. In fact, our experiments suggest that a 3:1 ratio of alpha A to alpha B subunit composition in an alpha-crystallin molecule is optimal in terms of thermal stability. This fascinating result explains the stoichiometric ratios of alpha A- and alpha B-crystallin subunits in the mammalian lens.
289586
The function of a protein depends on its shape.  If you alter the shape of it, you alter its function.  pH is a factor that can alter the shape, because the pKa values of residues on the protein will dictate which residues are or are not protonated, and that will, in turn, affect the manner in which the various amino acids will form internal ionic bonds.\n\nTemperature is another factor.  the stability of intramolecular bonding is dependent on the level of thermal excitation.  If a protein is at a high temperature, the thermal motion of the atoms might upset their abilities to form bonds.  At really high heat, the result will be total denaturation.  At low temperatures, you might even have the opposite problem, with a protein clinging to things in the wrong ways.\n\nFinally, you might alter it by introducing a chemical that reacts with it.  Some proteins need activator molecules to function, others might be inactivated by an inhibitor.  Enzymatic activity occurs in what is called the "active site" of the protein, which is where the substrates bind to the protein and catalysis occurs.  So the activity of the molecule might be altered by changing the arrangement of the moieties in the acive site relative to one another, of there might be a change which permits/blocks access to the active site by the substrate molecules.
578114
fluorescent microscopy will work for this.  First fix the cells (3% paraformaldehyde) then permeabilize (0.5% triton-x) and then stain with antibody to your protein of interest.
1171167
Try this , it really helped me in my first few lectures in cell bio , such as DNA and RNA . Loads of animations and stuff ! \n\nhttp://www.johnkyrk.com/DNAtranscription.html
613727
try:\nhttp://lb.chemie.uni-hamburg.de/static/data/50_zzk46n8n.html
677372
here are some useful sites visit them-\n\nhttp://www.stolaf.edu/people/hansonr/mo/x-ray.html\n\nhttp://news.uns.purdue.edu/html4ever/9804.Crystallography.html
1176807
Sounds like somebody is working on a biochem lab. :) \n\nDenaturation lowers enzyme activity because it changes the shape of the protein. Heat disrupts the tertiary structure by breaking covalent, non-covalent and van der waals interations between side chains of the protein. Proteins must be in the right conformation in order to perform their functions correctly. When they are denatured substrates can no longer bind to the active site, key amino acids are no longer in the correct position. \n\npH affects enzyme activity in the following ways: 1-enzyme binding to the active site 2-catalytic activity 3-ionization of the substrate 4-variation of protein structure. This is because pH will change the ionization state of certain side chains. (H+ ions will interact with \n\nOptimum conditions for alpha amylase (ptyalin) from wikipedia.com:\n Optimum pH-5.6 - 6.9\n Room temperatue- 37 degrees Celsius
237624
here's a basic answer about stuff we were recently talkin' about in class.... there are intrinsic and extrinsic proteins... also called integral and peripheral proteins... the first guys completely span the membrane bilayer and the second guys just touch the surface of the membrane or only partially go into it.  Proteins can diffuse laterally in the membrane.  They also decrease the fluidity of the membrane and increase its rigidity.  I believe it's oligosaccarides or carbohydrates can also bind to the proteins.  Most of the proteins function though as transporters.  There's so many transporters that that's a new questions in itself and i don't feel like the typing! ;)
709812
You can measure it in a number of ways depending on the protein.\n\n-- pH may vary directly with concentration\n-- optical rotation measurements may work for some\n-- adding a dye to the protein and reading on a colorimeter\n-- Another way would be to degrade or react the protein in solution and then to measure the byproducts of the degradation/reaction by something as simple as a titration
327822
Are you looking at any protein in particular?  Look up in situ hybrdization for proteins ( at least it will give you an idea where it is localised).  I think that it would really depend on the system ad proteins that you want to study, so I am not sure how much else I can tell you, sorry.