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Do all backbone polar groups in proteins form hydrogen bonds?
| Content Provider | Semantic Scholar |
|---|---|
| Author | Fleming, Patrick J. Rose, George D. |
| Copyright Year | 2005 |
| Abstract | Evidence from proteins and peptides supports the conclusion that intrapeptide hydrogen bonds stabilize the folded form of proteins. Paradoxically, evidence from small molecules supports the opposite conclusion, that intrapeptide hydrogen bonds are less favorable than peptide-water hydrogen bonds. A related issue-often lost in this debate about comparing peptide-peptide to peptide- water hydrogen bonds-involves the energetic cost of an unsatisfied hydrogen bond. Here, experiment and theory agree that breaking a hydrogen bond costs between 5 and 6 kcal/mol. Accordingly, the likelihood of finding an unsatisfied hydrogen bond in a protein is insignificant. This realization establishes a powerful rule for evaluating protein conformations. |
| Starting Page | 56 |
| Ending Page | 62 |
| Page Count | 7 |
| File Format | PDF HTM / HTML |
| Alternate Webpage(s) | http://w3.ualg.pt/~pmartel/cadeiras/be/papers/artigo_0.pdf |
| PubMed reference number | 15937286v1 |
| Volume Number | 14 |
| Issue Number | 7 |
| Journal | Protein science : a publication of the Protein Society |
| Language | English |
| Access Restriction | Open |
| Subject Keyword | DUOXA1 gene Hydrogen Bonding Instinct Polypeptides Pyschological Bonding Small Molecule Staphylococcal Protein A Vertebral column kilocalorie |
| Content Type | Text |
| Resource Type | Article |
