Conformational Profile of Bombesin and Its Mammalian Analogues - Sharma, Parul
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Understanding the dynamics and mechanism of protein folding continues to be one of the central problems in molecular biology. Peptide folding experiments characterize the dynamics and molecular mechanisms of the early events of protein folding. However, generally the highly flexible nature of peptides makes their bioactive conformation assessment reasonably difficult as peptides fold at very fast rates experimentally, requiring probing on the nanosecond time resolution. The present work focuses on the exploration of the conformational space of biologically active neuropeptides with the aim of…mehr

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Produktbeschreibung
Understanding the dynamics and mechanism of protein folding continues to be one of the central problems in molecular biology. Peptide folding experiments characterize the dynamics and molecular mechanisms of the early events of protein folding. However, generally the highly flexible nature of peptides makes their bioactive conformation assessment reasonably difficult as peptides fold at very fast rates experimentally, requiring probing on the nanosecond time resolution. The present work focuses on the exploration of the conformational space of biologically active neuropeptides with the aim of characterizing their conformational profile. Specifically, bombesin, neuromedin B (NMB) and neuromedin C (NMC), have been chosen for the current investigations. This study would help students and scientific community to understand the role of computational simulation techniques in the filed of conformational sampling and peptide folding.
Autorenporträt
Dr Parul Sharma, masters in organic chemistry and bioinformatics from Jamia Millia Islamia in New Delhi, has completed her PhD in computational Chemistry from Durban University of Technology in 2011. She has worked in the field of Peptide folding to understand the bioactive conformation of neuropeptides using computational simulation techniques.