Zobrazeno 1 - 10
of 14
pro vyhledávání: '"Venkatraman Ramanujam"'
Autor:
Gagan Sharma, Carolyne B. Braga, Kai-En Chen, Xinying Jia, Venkatraman Ramanujam, Brett M. Collins, Roberto Rittner, Mehdi Mobli
Publikováno v:
Current Research in Structural Biology, Vol 3, Iss , Pp 179-186 (2021)
Chlorotoxin (ClTx) is a 36-residue disulfide-rich peptide isolated from the venom of the scorpion Leiurus quinquestriatus. This peptide has been shown to selectively bind to brain tumours (gliomas), however, with conflicting reports regarding its dir
Externí odkaz:
https://doaj.org/article/af52d3404ddf4994b4ff881afbc923be
Publikováno v:
Frontiers in Chemistry, Vol 7 (2020)
Disulfide bridges in proteins are formed by the oxidation of pairs of cysteine residues. These cross-links play a critical role in stabilizing the 3D-structure of small disulfide rich polypeptides such as hormones and venom toxins. The arrangement of
Externí odkaz:
https://doaj.org/article/262204a7ccc34c8e85bc0f36f0f4177b
The structure, dynamics and selectivity profile of a NaV1.7 potency-optimised huwentoxin-IV variant.
Autor:
Sassan Rahnama, Jennifer R Deuis, Fernanda C Cardoso, Venkatraman Ramanujam, Richard J Lewis, Lachlan D Rash, Glenn F King, Irina Vetter, Mehdi Mobli
Publikováno v:
PLoS ONE, Vol 12, Iss 3, p e0173551 (2017)
Venom-derived peptides have attracted much attention as potential lead molecules for pharmaceutical development. A well-known example is Huwentoxin-IV (HwTx-IV), a peptide toxin isolated from the venom of the Chinese bird-eating spider Haplopelma sch
Externí odkaz:
https://doaj.org/article/df41c8b4e37143b68c0e5ea483a42562
Publikováno v:
PLoS ONE, Vol 9, Iss 4, p e94513 (2014)
Structural topology plays an important role in protein mechanical stability. Proteins with β-sandwich topology consisting of Greek key structural motifs, for example, I27 of muscle titin and (10)FNIII of fibronectin, are mechanically resistant as sh
Externí odkaz:
https://doaj.org/article/fae25d35d551497885c5de24917bd5fc
Autor:
Brett M. Collins, Mehdi Mobli, Venkatraman Ramanujam, Xinying Jia, Kai-En Chen, Carolyne B. Braga, Roberto Rittner, Gagan Sharma
Publikováno v:
Current Research in Structural Biology
Current Research in Structural Biology, Vol 3, Iss, Pp 179-186 (2021)
Current Research in Structural Biology, Vol 3, Iss, Pp 179-186 (2021)
Chlorotoxin (ClTx) is a 36-residue disulfide-rich peptide isolated from the venom of the scorpion Leiurus quinquestriatus. This peptide has been shown to selectively bind to brain tumours (gliomas), however, with conflicting reports regarding its dir
Publikováno v:
J Magn Reson
Pulsed-field gradient NMR spectroscopy is widely used to measure the translational diffusion and hydrodynamic radius (R(h)) of biomolecules in solution. For unfolded proteins, the R(h) provides a sensitive reporter on the ensemble-averaged conformati
Autor:
Sassan Rahnama, Mehdi Mobli, Jennifer R. Deuis, Fernanda C. Cardoso, Venkatraman Ramanujam, Lachlan D. Rash, Glenn F. King, Irina Vetter, Richard J. Lewis
Publikováno v:
PLoS ONE
PLoS ONE, Vol 12, Iss 3, p e0173551 (2017)
PLoS ONE, Vol 12, Iss 3, p e0173551 (2017)
Venom-derived peptides have attracted much attention as potential lead molecules for pharmaceutical development. A well-known example is Huwentoxin-IV (HwTx-IV), a peptide toxin isolated from the venom of the Chinese bird-eating spider Haplopelma sch
Autor:
Kandala V. R. Chary, Atul K. Srivastava, Venkatraman Ramanujam, Yogendra Sharma, Sunita Patel
Publikováno v:
Biomolecular NMR Assignments. 7:221-224
The sequence specific backbone (1)H, (13)C and (15)N resonance assignments of an intrinsically unstructured βγ-crystallin from Hahella chejuensis are reported. The secondary structure chracterization of the unstructured protein reveals that large f
Publikováno v:
Protein Expression and Purification. 84:116-122
βγ-Crystallins are a large superfamily of proteins found in vertebrate eye lens. They are hetero-dimers (linked in tandem by a specific peptide) and are shown to bind calcium. The monomers possess two β-strand rich greek-key motifs. Recently, a st
Autor:
Glenn F. King, Frank Bosmans, Graham M. Nicholson, Niraj S. Bende, Geoffrey W. Brown, Venkatraman Ramanujam, Sławomir Dziemborowicz, Mehdi Mobli, Volker Herzig
Publikováno v:
The FEBS journal. 282(5)
Spider venoms contain a plethora of insecticidal peptides that act on neuronal ion channels and receptors. Because of their high specificity, potency and stability, these peptides have attracted much attention as potential environmentally friendly in