Synthetic mimetics of protein secondary structure domains.
Proteins modulate the majority of all biological functions and are primarily composed of highly organized secondary structural elements such as helices, turns and sheets. Many of these functions are affected by a small number of key protein-protein contacts, often involving one or more of these well...
| Main Authors: | , , |
|---|---|
| Format: | Journal article |
| Language: | English |
| Published: |
2010
|
| _version_ | 1826272945744379904 |
|---|---|
| author | Ross, N Katt, W Hamilton, A |
| author_facet | Ross, N Katt, W Hamilton, A |
| author_sort | Ross, N |
| collection | OXFORD |
| description | Proteins modulate the majority of all biological functions and are primarily composed of highly organized secondary structural elements such as helices, turns and sheets. Many of these functions are affected by a small number of key protein-protein contacts, often involving one or more of these well-defined structural elements. Given the ubiquitous nature of these protein recognition domains, their mimicry by peptidic and non-peptidic scaffolds has become a major focus of contemporary research. This review examines several key advances in secondary structure mimicry over the past several years, particularly focusing upon scaffolds that show not only promising projection of functional groups, but also a proven effect in biological systems. |
| first_indexed | 2024-03-06T22:20:34Z |
| format | Journal article |
| id | oxford-uuid:54e82620-d6af-4f74-850e-62dd3460caa5 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-06T22:20:34Z |
| publishDate | 2010 |
| record_format | dspace |
| spelling | oxford-uuid:54e82620-d6af-4f74-850e-62dd3460caa52022-03-26T16:40:37ZSynthetic mimetics of protein secondary structure domains.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:54e82620-d6af-4f74-850e-62dd3460caa5EnglishSymplectic Elements at Oxford2010Ross, NKatt, WHamilton, AProteins modulate the majority of all biological functions and are primarily composed of highly organized secondary structural elements such as helices, turns and sheets. Many of these functions are affected by a small number of key protein-protein contacts, often involving one or more of these well-defined structural elements. Given the ubiquitous nature of these protein recognition domains, their mimicry by peptidic and non-peptidic scaffolds has become a major focus of contemporary research. This review examines several key advances in secondary structure mimicry over the past several years, particularly focusing upon scaffolds that show not only promising projection of functional groups, but also a proven effect in biological systems. |
| spellingShingle | Ross, N Katt, W Hamilton, A Synthetic mimetics of protein secondary structure domains. |
| title | Synthetic mimetics of protein secondary structure domains. |
| title_full | Synthetic mimetics of protein secondary structure domains. |
| title_fullStr | Synthetic mimetics of protein secondary structure domains. |
| title_full_unstemmed | Synthetic mimetics of protein secondary structure domains. |
| title_short | Synthetic mimetics of protein secondary structure domains. |
| title_sort | synthetic mimetics of protein secondary structure domains |
| work_keys_str_mv | AT rossn syntheticmimeticsofproteinsecondarystructuredomains AT kattw syntheticmimeticsofproteinsecondarystructuredomains AT hamiltona syntheticmimeticsofproteinsecondarystructuredomains |