Determination of Primary Amino Acid Sequence and Unique Three-Dimensional Structure of WGH1, a Monoclonal Human IgM Antibody with Anti-PR3 Specificity

1998 ◽  
Vol 89 (1) ◽  
pp. 35-43 ◽  
Author(s):  
Jacquelyn A. Davis ◽  
Elisabeth Peen ◽  
Ralph C. Williams ◽  
Shane Perkins ◽  
Christine C. Malone ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Three Dimensional ◽  
Dimensional Structure ◽  
Primary Amino Acid Sequence ◽  
Three Dimensional Structure ◽  
Igm Antibody ◽  
Primary Amino

scholarly journals Amino acid sequence and three-dimensional structure of the Tn-specific isolectin B4 fromVicia villosa

FEBS Letters ◽  
1997 ◽  
Vol 412 (1) ◽  
pp. 190-196 ◽  
Author(s):  
Eduardo Osinaga ◽  
Diana Tello ◽  
Carlos Batthyany ◽  
Mario Bianchet ◽  
Gisele Tavares ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Three Dimensional ◽  
Dimensional Structure ◽  
Three Dimensional Structure ◽  
Isolectin B4

Synopses from the poster exhibition organized by I. M. Kerr, 1. Interferon: a tertiary structure predicted from amino acid sequences

1982 ◽  
Vol 299 (1094) ◽  
pp. 125-127 ◽  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Tertiary Structure ◽  
Three Dimensional ◽  
Amino Acid Sequences ◽  
Dimensional Structure ◽  
X Ray ◽  
Three Dimensional Structure ◽  
X Ray Crystallography ◽  
Functional Studies

Functional studies on interferon would be helped by a three-dimensional structure for the molecule. However, it may be several years before the structure of the protein is determined by X-ray crystallography. We have therefore used available methods for predicting the secondary - and the tertiary - structure of a protein from its amino acid sequence to propose a tertiary model involving the packing of four a-helices. Details of this work have been published elsewhere (Sternberg & Cohen 1982).

scholarly journals Systematic construction and prediction of the arrangement of the strands of sandwich proteins

2008 ◽  
Vol 6 (30) ◽  
pp. 63-73 ◽  
Author(s):  
T.S Papatheodorou ◽  
A.S Fokas
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Large Class ◽  
A Priori ◽  
Three Dimensional ◽  
Direct Consequence ◽  
Dimensional Structure ◽  
Open Problems ◽  
Geometrical Structures ◽  
Three Dimensional Structure

The problem of predicting the three-dimensional structure of a protein starting from its amino acid sequence is regarded as one of the most important open problems in biology. Here, we solve aspects of this problem for the so-called sandwich proteins that constitute a large class of proteins consisting of only β-strands arranged in two sheets. A breakthrough for this class of proteins was announced in Kister et al . (Kister et al. 2002 Proc. Natl Acad. Sci. USA 99 , 14 137–14 141), in which it was shown that sandwich proteins contain a certain invariant substructure called interlock . It was later noted that approximately 90% of the observed sandwich proteins are canonical , namely they are generated by certain geometrical structures . Here, employing a topological investigation, we prove that interlocks and geometrical structures are the direct consequence of certain biologically motivated fundamental principles. Furthermore, we construct all possible canonical motifs involving 6–10 strands. This construction limits dramatically the number of possible motifs. For example, for sandwich proteins with nine strands, the a priori number of possible canonical motifs exceeds 360 000, whereas our construction yields only 49 geometrical structures and 625 canonical motifs.

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