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(pg. 1451- 1466) Google Scholar CrossRef Search ADS PubMed Broome BM, Hecht MH. Nature disfavors sequences of alternating polar and non - polar amino acids: implications for amyloidogenesis, J Mol ...
by ELISA. C. Logo plot depicting CDRH3 loop amino acid substitutions that maintained 10.17DT SOSIP binding (enrichment scores >-0.2). Non - polar residues are shown in black, polar residues in red and aromatic ...
contact prediction based on covariation to dramatically improve the accuracy of protein structure modeling [29]. Despite the clear occurrence of amino acid covariation in natural protein sequences ...
“complexity”, which is effectively a measure of the amino acid frequencies within a region of defined length. Most naturally -occurring proteins contain a rich mixture of residues drawn from the 20 canonical ...
; and third, in particular, the behavior of the parameters is a function of two factors: the extent of structural similarity between the two molecules and the sequence similarity. The non - polar buried surface ...
-FdUR resistant TS. Since 5-FdUMP is structurally similar to the natural substrate dUMP, it is difficult to predict how single amino acid substitutions or multiple substitutions could restrict the binding ...
] and experimentally confirmed [7] intrinsically disordered regions are available. Prediction of intrinsically disordered regions from primary amino acid sequences is a well-developed area of research in computational ...
. On the other hand, there is little sequence consensus up- and downstream of LPxY across the Nedd4 family, with a distribution of charged, polar , and non - polar residues present as highest probability residues ...
of substitutions in OaantCs with higher contact numbers has a stronger tendency of maintaining amino acid chemical properties, such as charge, hydropathy, and polarity . There are two factors that determine whether ...
that evolutionary selection has tended to avoid amino acid sequences , such as alternating polar and hydrophobic residues, that favor a β-sheet structure of the type seen in amyloid fibrils (Broome and Hecht 2000 ...
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