Sasidhar YU - Search Results

1

Loop propensity of the sequence YKGQP from staphylococcal nuclease: implications for the folding of nuclease.

Patel S, Sasidhar YU. Patel S, et al. Among authors: sasidhar yu. J Pept Sci. 2007 Oct;13(10):679-92. doi: 10.1002/psc.907. J Pept Sci. 2007. PMID: 17787022

2

Beta-hairpins with native-like and non-native hydrogen bonding patterns could form during the refolding of staphylococcal nuclease.

Patel S, Sista P, Balaji PV, Sasidhar YU. Patel S, et al. Among authors: sasidhar yu. J Mol Graph Model. 2006 Sep;25(1):103-15. doi: 10.1016/j.jmgm.2005.11.007. Epub 2005 Dec 28. J Mol Graph Model. 2006. PMID: 16386445

3

The sequence TGAAKAVALVL from glyceraldehyde-3-phosphate dehydrogenase displays structural ambivalence and interconverts between alpha-helical and beta-hairpin conformations mediated by collapsed conformational states.

Patel S, Balaji PV, Sasidhar YU. Patel S, et al. Among authors: sasidhar yu. J Pept Sci. 2007 May;13(5):314-26. doi: 10.1002/psc.843. J Pept Sci. 2007. PMID: 17437248

4

A small tripeptide AFA undergoes two state cooperative conformational transitions: implications for conformational biases in unfolded states.

Patel S, Taimni R, Sasidhar YU. Patel S, et al. Among authors: sasidhar yu. Protein Pept Lett. 2007;14(6):581-9. doi: 10.2174/092986607780989886. Protein Pept Lett. 2007. PMID: 17627600

5

A shorter peptide model from staphylococcal nuclease for the folding-unfolding equilibrium of a beta-hairpin shows that unfolded state has significant contribution from compact conformational states.

Patel S, Sasidhar YU. Patel S, et al. Among authors: sasidhar yu. J Struct Biol. 2008 Oct;164(1):60-74. doi: 10.1016/j.jsb.2008.06.003. Epub 2008 Jun 15. J Struct Biol. 2008. PMID: 18602478

6

Molecular dynamics simulations of certain mutant peptide models from staphylococcal nuclease reveal that initial hydrophobic collapse associated with turn propensity drives β-hairpin folding.

Shukla RT, Kumar N, Sasidhar YU. Shukla RT, et al. Among authors: sasidhar yu. J Pept Sci. 2013 Aug;19(8):516-27. doi: 10.1002/psc.2530. Epub 2013 Jun 21. J Pept Sci. 2013. PMID: 23794524

7

Mechanism of Initiation, Association, and Formation of Amyloid Fibrils Modeled with the N-Terminal Peptide Fragment, IKYLEFIS, of Myoglobin G-Helix.

Patel S, Sasidhar YU, Chary KVR. Patel S, et al. Among authors: sasidhar yu. J Phys Chem B. 2017 Aug 17;121(32):7536-7549. doi: 10.1021/acs.jpcb.7b02205. Epub 2017 Aug 3. J Phys Chem B. 2017. PMID: 28707888

8

Conformational features of a peptide model Ac-DTVKLMYKGQPMTFR-NH2, corresponding to an early folding beta hairpin region of staphylococcal nuclease.

Ramakrishna V, Sasidhar YU. Ramakrishna V, et al. Among authors: sasidhar yu. Indian J Biochem Biophys. 1998 Dec;35(6):333-8. Indian J Biochem Biophys. 1998. PMID: 10412226

9

A pentapeptide model for an early folding step in the refolding of staphylococcal nuclease: the role of its turn propensity.

Ramakrishna V, Sasidhar YU. Ramakrishna V, et al. Among authors: sasidhar yu. Biopolymers. 1997 Feb;41(2):181-91. doi: 10.1002/(SICI)1097-0282(199702)41:2<181::AID-BIP5>3.0.CO;2-P. Biopolymers. 1997. PMID: 9004552

10

For the sequence YKGQ, the turn and extended conformational forms are separated by small barriers and the turn propensity persists even at high temperatures: implications for protein folding.

Kaur H, Sasidhar YU. Kaur H, et al. Among authors: sasidhar yu. J Phys Chem B. 2012 Mar 29;116(12):3850-60. doi: 10.1021/jp210227s. Epub 2012 Mar 16. J Phys Chem B. 2012. PMID: 22385393

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