Sequence Chain View tassiu Site Rec Pretein Medification AL HWRAAGAATVLLVIVLLAGS
ID: 187529 • Letter: S
Question
Sequence Chain View tassiu Site Rec Pretein Medification AL HWRAAGAATVLLVIVLLAGSYLAVLAERGAPGAOLITYPRAL WWS VETATTVGYGDLY PDE 70 to s2 scor Potassium Channel protein (dibl8a Site Rec Protein VTL WGR CVAVVVMVAGITSFGLVTAALATWF VGRE Q 115 90 100 Protein Modification Legend potassium ion - + -potassium ion Site Record Legend O FILTER TO SELECT FOR POTASSIUM IONS OVER OTHER MONOVALENT CATIONS. (Author) BINDING SITE FOR RESIDUE KA 401 (Software BINDING SITE FOR RESIDUE K A 402 (Software) DSSP Legend empty no secondary structure assigned -S: bend H: alpha helx Estimate the length of each alpha-helical segment and compare it to the thickness of a biological membrane. A good estimate for the thickness of a cell membrane can be found at http://book.bionumbers.org/what-is-the-thickness-of-the-cell-membrane/. Don't forget that 1Explanation / Answer
generally the thickness of biological memberane are 5 to 8 nm thick. Memberane are semioermeable structure. In case of plasma memberane Iligopeptide readily adopt stable alpha helical structure.Alpha helix structure show the secondary structure of protein having spiral form> the backbone contain strng hydrogen bond, in which N-H group is hydrogen bonded C=O group of amino acid. The protein to lipid ratio in memberane is always greater than one.
In case of biological memberane pottasium channel control transportation of pottasium ions. pottasium channel have helices consist of lipid bilayer. It is divided into two forms naming pore forming domain and regulatory domain.pore forming domain is responsible for transportattion of K+ ion however regulatory domain senses different stimuli.
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