Untangling influences of hydrophobicity on protein sequences and structures

Details Untangling influences of hydrophobicity on protein sequences and structures Untangling influences of hydrophobicity on protein sequences and structures

2004-06-08

arxiv.org/abs/q-bio/0406019v1

Biology

Quantitative Biology

Biomolecules

4 pages, 3 figures, 7 eps files

Scientific paper

We fit the Fourier transforms of solvent accessibility and hydrophobicity profiles of a representative set of proteins to a joint multi-variable Gaussian. This allows us to separate the intrinsic tendencies of sequence and structure profiles from the interactions that correlate them; for example, the $\alpha$-helix periodicity in sequence hydrophobicity is dictated by the solvent accessibility of structures. The distinct intrinsic tendencies of sequence and structure profiles are most pronounced at long periods, where sequence hydrophobicity fluctuates more, while solvent accessibility fluctuations are less than average. Interestingly, correlations between the two profiles can be interpreted as the Boltzmann weight of the solvation energy at room temperature.

Affiliated with

Also associated with

No associations

Rating

Untangling influences of hydrophobicity on protein sequences and structures does not yet have a rating. At this time, there are no reviews or comments for this scientific paper.

If you have personal experience with Untangling influences of hydrophobicity on protein sequences and structures, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Untangling influences of hydrophobicity on protein sequences and structures will most certainly appreciate the feedback.

Rate now

Comments { 0 }

Profile ID: LFWR-SCP-O-719427