Isoelectric point of protein?
965402
The protein will be negatively charged because th high pH of the solution cause the solution to have a high hydroxide concentration (relatively) and will cause extraction of hydrogen atoms from acidic residues on the aminio acids of the protein.  I would use a weak anion exchanger for the ion exchange chromatography of this protein.
527995
Particles, Amino acids (compounds), Proteins, Cells is as specific as I can get.  Seems this question is incomplete.
910706
so you plot the proton number on the y-axis, and the different melting points of the elements across the x- axis.. actually are sure it has to be a bar graph.. i think a line/scatter graph would be more accurate maybe?
885040
the building blocks of protein
654853
Use a Bradford assay for protein. This uses a dye which goes from red to blue when it binds to proteins, and the colour change and hence the amount of protein present cana be assessed spectrophotometrically. This is a cheap, sensitive method and will give you a quantitative answer (providing you calibrate your spectrophotometer first using a standard curve produced with solutions of different known protein concentrations). This link will tell you more about the exact method.\n\nhttp://www-class.unl.edu/biochem/protein_assay/bradford_assay.htm
936998
a) isotonic to the blood
81856
All answers are correct. The primary aminoacid sequence is changed which may have implications for the structure and funtion of the protein
158656
Unable to guesstimate.  You're talking biological macromolecules, most likely.  They would probably have carbon, hydrogen, nitrogen, oxygen, sulfur, phosphorus, and perhals a halogen or two.  And maybe even a metal ion or two thrown in for good measure.
901348
well let me think...ITS A DOUBLE HELIX!!!!!!!!!!!!\nDOUBLE          DOUBLE               DOUBLE
722594
I think most theoretical chemists would agree that the holy grail in the field would be accurate prediction of folded protein structure using only the primary amino acid sequence. \n\nWhat makes this difficult is the enormous size of proteins, the numerous non-bonded interactions, and the necessity to model solvent interactions with chemical accuracy. Even with accurate methods to do a single point energy calculation, you still have to find methods to effectively serach the conformational space to locate the global energy minimum. It's a big problem, and would definitely be worth a Nobel prize.
593819
It appears that the constants are calculated at one condition (dry,wet,etc) whereas the effective is closer to reality.  See\n\nhttp://www.pnas.org/cgi/content/full/102/45/16293
277411
What a wonderfully esoteric question!  I've been able to find one site (or a doc on a site) that says,\n\n"The effective spring constant of the DNA is 0.073 pN/nm .."\nhttp://picasso.ucsf.edu/~mollyd/ProblemSet2.doc\n\nBut, I don't know if this will meet your needs.  Here's my search terms.  Maybe you can browse these hits and see if something is more appropriate.\n\nhttp://www.google.com/search?q=dna+%22spring+constant%22+pN/nm+&hl=en&lr=&rls=GGLJ,GGLJ:2006-08,GGLJ:en&start=30&sa=N
294618
Arginine being an aminoacid has a COOH terminus and an NH3 terminus.\nat Ph 7(also called "isoelectric Ph"),all aminoacids become amphoteric.ie,they have both +ve and -ve charge due to ionization of COOH into COO- and NH3 into NH3+.so,when it is protonated,obviously it's COO- group gets neutralized(since proton is added)and gets converted to COOH and now arginine is left with the +vely charged NH3+ grp.THUS it acts as a base.
285539
a lot. There are innumerable myoglobin molecules per myofibril, so I do not think that can be measured
215160
http://www-ec.njit.edu/~skawinsk/chem243/chap11/chap11.htm\nthis may help–near the bottom
4139
Whey protein is one of the highest quality proteins.  Protein quality is measured based on the amino acid composition of the protein in comparison with the amino acid proportions the body needs.  Egg is generally considered to have a quality of 100%, and some lecture notes I was given for my med school biochem class put whey protein at second best at about 93%.
132965
When doing certain spectrophotometric assays, you can determine that proteins have a maximal absorbance at 260 nm, while DNA has a maximal absorbance at 280 nm (I just can't remember which assay it is...Biuret maybe?). \n\nAnyway point is...if the ratio of 260/280 is much greater than 1, you probably have DNA. If the ratio of 260/280 is much less than 1, you probably have RNA. If it is about 1, you probably have both.