Publications by authors named "Somayyeh Hoseini"
Due to the slightly success of protein secondary structure prediction using the various algorithmic and non-algorithmic techniques, similar techniques have been developed for predicting gamma-turns in proteins by Kaur and Raghava [2003. A neural-network based method for prediction of gamma-turns in proteins from multiple sequence alignment. Protein Sci.
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- A systematic analysis was conducted to explore how specific parameters contribute to the adaptation of proteins to cold environments.
- The study found that certain structural properties, such as residual structure states and secondary structure states, are similar in both cold-adapted (psychrophilic) and normal-temperature (mesophilic) proteins.
- Additionally, the research revealed new patterns in amino acid preferences for cold adaptation, suggesting potential strategies for designing proteins that function in low-temperature conditions.
In order to investigate the structural distribution responsible for protein psychrophilicity, a systematic comparative analysis of 13 pairs of psychrophilic and mesophilic proteins is reported. Three kinds of residue structural states such as exposed, intermediate and buried were considered for analyzing the structural patterns of single amino acids and amino acids in different groups. The statistical test revealed that higher frequency in exposed state of Ala, higher frequency in intermediate state of His, lower frequency in buried state of Lys, lower frequency in exposed state of Gln, higher frequency in exposed state and in intermediate state of Thr, higher frequency in exposed and intermediate state of tiny and small amino acids groups could be critical factors related with protein psychrophilicity.
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