Abstract
The solvent‐accessible surface areas (ASAs), of the atoms in tripeptides around the minimum‐energy conformations of the β‐bend types I, I′, II, and II′ have been computed as a first step in the systematic solvent accessibiity study of secondary structures. The side chains chosen at the two middle positions of the bend are L‐Ala, D‐Ala, and Gly. The ASAs of the hydrogen atoms are reported here and are found useful in determining the type of β‐bends in six examples of cyclic hexapeptides whose crystal structures are known. Comparison with observation showed that all the β‐bends in these cyclic hexapeptides were correctly identified by the present method. This points to a possible use of the method in identifying β‐bend types in solution.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 1205-1214 |
| Number of pages | 10 |
| Journal | Biopolymers |
| Volume | 24 |
| Issue number | 7 |
| DOIs | |
| State | Published - 1985 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Biophysics
- Biochemistry
- Biomaterials
- Organic Chemistry
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Solvent accessibility studies of β‐bends and application to cyclic hexapeptides. / Soman, K. V.; Ramakrishnan, C.
In: Biopolymers, Vol. 24, No. 7, 1985, p. 1205-1214.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Solvent accessibility studies of β‐bends and application to cyclic hexapeptides
AU - Soman, K. V.
AU - Ramakrishnan, C.
PY - 1985
Y1 - 1985
N2 - The solvent‐accessible surface areas (ASAs), of the atoms in tripeptides around the minimum‐energy conformations of the β‐bend types I, I′, II, and II′ have been computed as a first step in the systematic solvent accessibiity study of secondary structures. The side chains chosen at the two middle positions of the bend are L‐Ala, D‐Ala, and Gly. The ASAs of the hydrogen atoms are reported here and are found useful in determining the type of β‐bends in six examples of cyclic hexapeptides whose crystal structures are known. Comparison with observation showed that all the β‐bends in these cyclic hexapeptides were correctly identified by the present method. This points to a possible use of the method in identifying β‐bend types in solution.
AB - The solvent‐accessible surface areas (ASAs), of the atoms in tripeptides around the minimum‐energy conformations of the β‐bend types I, I′, II, and II′ have been computed as a first step in the systematic solvent accessibiity study of secondary structures. The side chains chosen at the two middle positions of the bend are L‐Ala, D‐Ala, and Gly. The ASAs of the hydrogen atoms are reported here and are found useful in determining the type of β‐bends in six examples of cyclic hexapeptides whose crystal structures are known. Comparison with observation showed that all the β‐bends in these cyclic hexapeptides were correctly identified by the present method. This points to a possible use of the method in identifying β‐bend types in solution.
UR - http://www.scopus.com/inward/record.url?scp=84990438213&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84990438213&partnerID=8YFLogxK
U2 - 10.1002/bip.360240708
DO - 10.1002/bip.360240708
M3 - Article
AN - SCOPUS:84990438213
VL - 24
SP - 1205
EP - 1214
JO - Biopolymers
JF - Biopolymers
SN - 0006-3525
IS - 7
ER -