Residue number system

Amino acid sequences of Type 1 sea anemone polypeptides. The residue numbering system is based on the sequences of AP-A and AP-B. Literature references are from Norton [24], except in the case of recently published sequences for Be III [25], Bg II and Bg III... 

Having assembled the backbone structures of collagens I and II, specific amino acid side chains may be added. In particular, the incorporation of the Gly.Pro.Hypro sequence (which contributed to the downfall of so many previous models) must be considered. Table VII summarizes the possible positions of various types of side chains in terms of the residue numbering system used in Fig. 10. 

Both word-level and bit-level parallelism should be exploited to reach the extreme throughputs which are needed in particular applications like radar processing [33]. Extensions in this direction are introduced in chapter 5. Employing the features of various arithmetic systems, such as 2 s complement and residue number systems (RNS) [42], bit-level systolic arrays can now be derived automatically. 

V. Paliouras, D. Soudris, and T. Stouraitis. Systematic derivation of the processing element of a systolic array based on residue number system. Proc. IEEE Ini. Symp. on Circuits and Systems, San Diego, CA, 1992. 

Table. Abnormal hemoglobins. The names of abnormal hemoglobins usually refer to the geographical location where the hemoglobin was first discovered. The term, unstable, refers to those hemoglobins associated with accelerated erythrocyte destruction in vivo and precipitation of hemoglobin in vitro when warm to SOX. For residue numbering system and comparison with normal hemoglobin A, see Hemoglobin.

A basic understanding of the structure of the BCR-ABLl chimeric protein is important to understanding how the multiple mutations that have been described in the ABLl kinase domain cause resistance. The c-ABLl protein is expressed in two splice forms that are known as la and lb (Fig. 1C). The la form is 19 residues shorter than lb. The lb form contains a myristoylation site on its second residue. The second residue is a glycine that appears to help regulate enzymatic activity, and its mutations to alanine prevents myristoylation and results in an activated kinase (50). The lb form also contains a cap region that is believed to stabilize the inactive eonfirmation of the kinase (51). The numbering system used to identify the amino acid residues where mutations occur is based on the shorter la form. 

This tetrameric enzyme (subunit 36000) has been the subject of several crystallographic studies (summarized in [55]), and information on the dogfish isozyme has been obtained at high resolution [78]. The subunit structure [79] is illustrated in Fig. 18. On the basis of crystallographic findings, a numbering system for the amino acid chain was introduced [80], and has been widely used [55,79,81]. What were already known as Ser-163, Arg-171 and His-195 would simply become Ser-161, Arg-169 and His-193 in the consecutively numbered complete sequence [82]. However, in other parts of the chain (notably around residue 33, residue 187, and the regions 135-147 and 236-252) there were more extensive differences. For simplicity,... 

---