2007-02-05 06:19:16 · 4 answers · asked by jon & Corrie A 1 in Science & Mathematics ➔ Chemistry
By heating; treatment with acid, base, organic solven, or concentrated aqueous urea. Anything that disrupts the hydrogen bonding, salt bridges, or dipole interactions, thus messing up the folding of the protein chain.
2007-02-05 06:25:03 · answer #1 · answered by steve_geo1 7 · 0⤊ 0⤋
This question is unclear.
You can denature proteins with heat, acid, some solvents.
When proteins are denatured the amino acids are unfolded, or more exactly they are refolded into new, non-active forms.
Does this help?
2007-02-05 06:24:06 · answer #2 · answered by Cindy B 5 · 0⤊ 0⤋
In quaternary structure denaturation, protein sub-units are dissociated and/or the spatial arrangement of protein subunits is disrupted.
Tertiary structure denaturation involves the disruption of:
Covalent interactions between amino acid side chains (such as disulfide bridges between cysteine groups). Noncovalent dipole-dipole interactions between polar amino acid side chains (and the surrounding solvent). Van der Waals (induced dipole) interactions between nonpolar amino acid side chains.
In secondary structure denaturation, proteins lose all regular repeating patterns such as alpha-helixes and beta-pleated sheets, and adopt a random coil configuration.
ref:
http://en.wikipedia.org/wiki/Denaturation_%28biochemistry%29
2007-02-05 06:23:44 · answer #3 · answered by Dr Dave P 7 · 0⤊ 0⤋
heat them
never seen an egg become solid ?
2007-02-05 06:23:47 · answer #4 · answered by scientific_boy3434 5 · 0⤊ 0⤋