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Extended Conformations of Polypeptides and Proteins in Urea and Guanidine Hydrochloride
| Content Provider | Semantic Scholar |
|---|---|
| Author | Krimm, Samuel |
| Copyright Year | 2003 |
| Abstract | By analyzing the effect of urea and guanidine hydrochloride on the circular dichroism of many polypeptides and proteins, it is concluded that under conditions of high concentration of the perturbant and a t low temperatures the resultant state approached is that of a local extended helix structure instead of a completely random coil. Intensification by urea and guanidine hydrochloride of the circular dichroism bands of poly-b proline I1 leads to the proof that the mechanism of interaction of urea and guanidine hydrochloride with proteins is through hydrogen bonding to the backbone carbonyl group. |
| File Format | PDF HTM / HTML |
| Alternate Webpage(s) | https://deepblue.lib.umich.edu/bitstream/handle/2027.42/37834/360120310_ftp.pdf;jsessionid=CB11DC631319C93216FCCA15A67E58DD?sequence=1 |
| Language | English |
| Access Restriction | Open |
| Subject Keyword | Bands Circular Dichroism Cold Temperature Guanidine Hydrochloride Hydrogen Bonding Internet backbone Poly A Polypeptides Procollagen-Proline Dioxygenase Proline Pyschological Bonding Resultant Urea Vertebral column adenotonsillectomy |
| Content Type | Text |
| Resource Type | Article |