Primary structure and function of novel O-glycosylated hirudins from the leech Hirudinaria manillensis

Biochemistry ◽  
1992 ◽  
Vol 31 (8) ◽  
pp. 2294-2298 ◽  
Author(s):  
Verena Steiner ◽  
Rene Knecht ◽  
K. Olaf Boernsen ◽  
Ernst Gassmann ◽  
Stuart R. Stone ◽  
...  
Keyword(s):  
Primary Structure ◽  
Structure And Function ◽  
And Function

scholarly journals Primary structure and function of a cytotoxic outer-membrane protein (ComP) of Plesiomonas shigelloides

2008 ◽  
Vol 281 (1) ◽  
pp. 10-16 ◽  
Author(s):  
Hitoshi Tsugawa ◽  
Asako Ogawa ◽  
Satomi Takehara ◽  
Mayumi Kimura ◽  
Yoshio Okawa
Keyword(s):  
Membrane Protein ◽  
Outer Membrane ◽  
Outer Membrane Protein ◽  
Primary Structure ◽  
Structure And Function ◽  
Plesiomonas Shigelloides ◽  
And Function

scholarly journals Evolutionary conservation of P-selectin glycoprotein ligand-1 primary structure and function

2007 ◽  
Vol 7 (1) ◽  
pp. 166 ◽  
Author(s):  
Bénédicte Baïsse ◽  
Frédérique Galisson ◽  
Sylvain Giraud ◽  
Marc Schapira ◽  
Olivier Spertini
Keyword(s):  
Primary Structure ◽  
Evolutionary Conservation ◽  
Structure And Function ◽  
And Function

scholarly journals Erratum

2000 ◽  
Vol 65 (8) ◽  
pp. 609-609
Author(s):  
E Editorial
Keyword(s):  
Alcohol Dehydrogenase ◽  
Primary Structure ◽  
Structure And Function ◽  
Yeast Alcohol Dehydrogenase ◽  
And Function ◽  
Font Color

Erratum In the paper entitled "Structure and Function of Yeast Alcohol Dehydrogenase" by Svetlana Trivic and Vladimir Leskovac published in J. Serb. Chem. Soc. Vol. 65. No. 4 (2000) Table 5 on page 213 should be replaced with: TABLE V. Primary structure of the three isoenzymes of yeast alcohol dehydrogenase. <br><br><font color="red"><b> Link to the corrected article <u><a href="http://dx.doi.org/10.2298/JSC0004207T">10.2298/JSC0004207T</a></b></u>

scholarly journals Structure and function of yeast alcohol dehydrogenase

2000 ◽  
Vol 65 (4) ◽  
pp. 207-227 ◽  
Author(s):  
Svetlana Trivic ◽  
Vladimir Leskovac
Keyword(s):  
Alcohol Dehydrogenase ◽  
Substrate Specificity ◽  
Primary Structure ◽  
Active Site ◽  
Hydride Transfer ◽  
Kinetic Mechanism ◽  
Structure And Function ◽  
Chemical Mechanism ◽  
And Function ◽  
Font Color

1. Introduction 2. Isoenzymes of YADH 3. Substrate specificity 4. Kinetic mechanism 5. Primary structure 6. The active site 7. Mutations in the yeast enzyme 8. Chemical mechanism 9. Binding of coenzymes 10. Hydride transfer <br><br><font color="red"><b> This article has been corrected. Link to the correction <u><a href="http://dx.doi.org/10.2298/JSC0008609E">10.2298/JSC0008609E</a><u></b></font>

scholarly journals Local frustration around enzyme active sites

2019 ◽  
Vol 116 (10) ◽  
pp. 4037-4043 ◽  
Author(s):  
Maria I. Freiberger ◽  
A. Brenda Guzovsky ◽  
Peter G. Wolynes ◽  
R. Gonzalo Parra ◽  
Diego U. Ferreiro
Keyword(s):  
Primary Structure ◽  
Active Sites ◽  
Protein Sequences ◽  
Structure And Function ◽  
Energy Landscapes ◽  
Biological Functions ◽  
Complex Energy ◽  
Oligomeric State ◽  
Catalytic Sites ◽  
And Function

Conflicting biological goals often meet in the specification of protein sequences for structure and function. Overall, strong energetic conflicts are minimized in folded native states according to the principle of minimal frustration, so that a sequence can spontaneously fold, but local violations of this principle open up the possibility to encode the complex energy landscapes that are required for active biological functions. We survey the local energetic frustration patterns of all protein enzymes with known structures and experimentally annotated catalytic residues. In agreement with previous hypotheses, the catalytic sites themselves are often highly frustrated regardless of the protein oligomeric state, overall topology, and enzymatic class. At the same time a secondary shell of more weakly frustrated interactions surrounds the catalytic site itself. We evaluate the conservation of these energetic signatures in various family members of major enzyme classes, showing that local frustration is evolutionarily more conserved than the primary structure itself.

scholarly journals Primary structure and function of a second essential member of the heterooligomeric TCP1 chaperonin complex of yeast, TCP1 beta.

1994 ◽  
Vol 91 (7) ◽  
pp. 2743-2747 ◽  
Author(s):  
D. Miklos ◽  
S. Caplan ◽  
D. Mertens ◽  
G. Hynes ◽  
Z. Pitluk ◽  
...  
Keyword(s):  
Primary Structure ◽  
Structure And Function ◽  
And Function
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