Alpha helices on the surface of proteins play a key role during hydrophobic collapse, a process involved in protein folding. In this context, the hydrophobic core forms as non-polar amino acids cluster together to avoid the aqueous environment. Meanwhile, alpha helices located on the surface tend to expose their polar residues, which helps stabilize the protein's folded structure by interacting with the aqueous environment. This spatial arrangement minimizes unfavorable interactions between hydrophobic regions and water, facilitating a more compact and energetically favorable conformation during folding.

Means alpha helix behave as hydrophobic and Hydrophilic property

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If the professor's name is only mentioned in the "Institute Fellowship" section and not in the "JRF" section, it usually indicates that the professor is associated with students funded directly through the institute's fellowship program rather than external fellowships like CSIR. However, in most cases, a candidate with a JRF can still apply to work under such professors, as long as the professor is willing to supervise JRF students. The important point is to directly communicate with the professor or the department to confirm whether they accept JRF-funded students. If they do, you can use your CSIR JRF fellowship to work under that professor, even if their name is listed only in the institute fellowship section.

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Thank you for your feedback! I understand the importance of providing explanations in English to ensure that everyone, including students from South India, can easily follow and prepare for competitive exams. I'll keep that in mind to help students grasp concepts better. Feel free to ask any questions, and I'll make sure the explanations are clear and helpful!

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