Zobrazeno 1 - 10
of 97
pro vyhledávání: '"Narayanaswamy, Shamala"'
Autor:
Narayanaswamy Shamala, Kamanna Kantharaju, Krishnayan Basuroy, Padmanabhan Balaram, Subrayashastry Aravinda
Publikováno v:
Amino Acids. 51:1297-1306
Gamma-aminobutyric acid (GABA, gammaAbu), an unsubstituted gamma-amino acid, is an important inhibitory neurotransmitter in the mammalian brain. The role of GABA in the treatment of epilepsy has triggered a great deal of interest in substituted gamma
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9a4bf126efd03c0304aa80812a647b67
https://doi.org/10.1007/s00726-019-02768-5
https://doi.org/10.1007/s00726-019-02768-5
Autor:
Krishnayan, Basuroy, Kamanna, Kantharaju, Subrayashastry, Aravinda, Narayanaswamy, Shamala, Padmanabhan, Balaram
Publikováno v:
Amino acids. 51(9)
Gamma-aminobutyric acid (GABA, gammaAbu), an unsubstituted gamma-amino acid, is an important inhibitory neurotransmitter in the mammalian brain. The role of GABA in the treatment of epilepsy has triggered a great deal of interest in substituted gamma
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::aea4b84bd594c512ca0fdec8a5864401
https://pubmed.ncbi.nlm.nih.gov/31428911
https://pubmed.ncbi.nlm.nih.gov/31428911
Publikováno v:
Journal of Peptide Science. 22:166-173
The crystal structure of a tripeptide Boc-Leu-Val-Ac12 c-OMe (1) is determined, which incorporates a bulky 1-aminocyclododecane-1-carboxylic acid (Ac12 c) side chain. The peptide adopts a semi-extended backbone conformation for Leu and Val residues,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::cb499fcffd29b24b3e570d08befe30d7
https://doi.org/10.1002/psc.2854
https://doi.org/10.1002/psc.2854
Autor:
Narayanaswamy Shamala, Indranil Saha
Publikováno v:
Biopolymers. 99:605-610
In the current study, the puckering states of the Proline ring occurring in diproline segments ((L) Pro-(L) Pro) in proteins has been investigated with a segregation made on the basis of cis and trans states for the Pro-Pro peptide bond and the confo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ea0ee58fa6d92bde2ce18f1afc6f16f0
https://doi.org/10.1002/bip.22224
https://doi.org/10.1002/bip.22224
Autor:
Appavu Rajagopal, Srinivasarao Raghothama, Narayanaswamy Shamala, Padmanabhan Balaram, Subrayashastry Aravinda
Publikováno v:
Biopolymers. 98:185-194
Crystal structures of eight peptide β-hairpins in the sequence Boc-Leu-Phe-Val-Xxx-Yyy-Leu-Phe-Val-OMe revealed that the Phe(2) and Phe(7) aromatic rings are in close spacial proximity, with the centroid–centroid distance (Rcen) of 4.4–5.4 A bet
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::594ff162f5aafc384fdae1fb08869c8e
https://doi.org/10.1002/bip.22003
https://doi.org/10.1002/bip.22003
Autor:
Indranil Saha, Narayanaswamy Shamala
Publikováno v:
Biopolymers. 97:54-64
The covalent linkage between the side-chain and the backbone nitrogen atom of proline leads to the formation of the five-membered pyrrolidine ring and hence restriction of the backbone torsional angle phi to values of -60 degrees +/- 30 degrees for t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2baafcc56cf4cb733d5319e649bdae7a
https://doi.org/10.1002/bip.21703
https://doi.org/10.1002/bip.21703
Publikováno v:
Biopolymers. 98:76-86
An 18-residue sequence Boc-Aib-Val-Ala-Leu-Aib-Val-Ala-Leu-Gly-Pro-Val-Ala-Leu-Aib-Val-Ala-Leu-Aib-OMe (UK18) was designed to examine the effect of introducing a Gly-Pro segment into the middle of a potentially helical peptide. The crystal structures
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::48f624905c5495e55965279d1a61f044
https://doi.org/10.1002/bip.21697
https://doi.org/10.1002/bip.21697
Publikováno v:
Accounts of Chemical Research. 42:1628-1639
Nature has used the all-alpha-polypeptide backbone of proteins to create a remarkable diversity of folded structures. Sequential patterns of 20 distinct amino adds, which differ only in their side chains, determine the shape and form of proteins. Our
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4d7b28fe585e97c36b4578d253e7e16e
https://doi.org/10.1021/ar9001153
https://doi.org/10.1021/ar9001153
Autor:
Srinivasarao Raghothama, Narayanaswamy Shamala, Padmanabhan Balaram, Sunanda Chatterjee, Chandrasekharan Ramakrishnan, Prema G. Vasudev
Publikováno v:
Journal of the American Chemical Society. 131:5956-5965
Hybrid peptide segments containing contiguous alpha and gamma amino acid residues can form C(12) hydrogen bonded turns which may be considered as backbone expanded analogues of C(10) (beta-turns) found in alphaalpha segments. Exploration of the regul
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::be66fe9645a2aa3d94c5e8fca167a823
https://doi.org/10.1021/ja900618h
https://doi.org/10.1021/ja900618h
Publikováno v:
International Journal of Peptide and Protein Research. 48:209-214
A diastereomeric mixture of the tripeptide Boc-Ala-Ile-Aib-OMe crystallized in the space group P1 from CH3OH/H2O. The unit cell parameters are a = 10.593(2) A, b = 14.377(3) A, c = 17.872(4) A, alpha = 104.41(2) degrees, beta = 90.55(2) degrees, gamm
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ed919f38f8f49a3c35cda57339c07dc4
https://doi.org/10.1111/j.1399-3011.1996.tb00833.x
https://doi.org/10.1111/j.1399-3011.1996.tb00833.x