Literature DB >> 7030620

Semisynthetic peptides and proteins.

I M Chaiken.   

Abstract

Semisynthesis provides a flexible approach for using chemical synthesis to produce large, biologically active polypeptides and analogues. Currently developing improvements in the basic methods used, including polypeptide fragmentation, peptide synthesis, and reconstitution of synthetic and native components, make this overall approach applicable to a variety of species. Sequence modification through semisynthesis thus provides a flexible route to explore the code of rules whereby primary structure directs higher order properties of folded conformation and biological function of large peptides and proteins. The fruits of this endeavor, an understanding of how these macromolecules work, and therein, a basis for design of new structures that ultimately may be produced directly or by recombinant DNA methods, have begun to emerge.

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Year:  1981        PMID: 7030620     DOI: 10.3109/10409238109108703

Source DB:  PubMed          Journal:  CRC Crit Rev Biochem        ISSN: 0045-6411


  12 in total

1.  An enigmatic peptide ligation reaction: protease-catalyzed oligomerization of a native protein segment in neat aqueous solution.

Authors:  S Kumaran; D Datta; R P Roy
Journal:  Protein Sci       Date:  2000-04       Impact factor: 6.725

2.  Use of enzymes in peptide synthesis.

Authors:  I M Chaiken; A Komoriya; M Ohno; F Widmer
Journal:  Appl Biochem Biotechnol       Date:  1982-09       Impact factor: 2.926

3.  Role of the amino-terminal region of streptokinase in the generation of a fully functional plasminogen activator complex probed with synthetic peptides.

Authors:  D Nihalani; R Kumar; K Rajagopal; G Sahni
Journal:  Protein Sci       Date:  1998-03       Impact factor: 6.725

4.  Crystallographic structure of an active, sequence-engineered ribonuclease.

Authors:  H C Taylor; A Komoriya; I M Chaiken
Journal:  Proc Natl Acad Sci U S A       Date:  1985-10       Impact factor: 11.205

5.  Site-specific incorporation of biophysical probes into proteins.

Authors:  V W Cornish; D R Benson; C A Altenbach; K Hideg; W L Hubbell; P G Schultz
Journal:  Proc Natl Acad Sci U S A       Date:  1994-04-12       Impact factor: 11.205

6.  Single amino acid substitutions influencing the folding pathway of the phage P22 tail spike endorhamnosidase.

Authors:  M H Yu; J King
Journal:  Proc Natl Acad Sci U S A       Date:  1984-11       Impact factor: 11.205

7.  Subtiligase: a tool for semisynthesis of proteins.

Authors:  T K Chang; D Y Jackson; J P Burnier; J A Wells
Journal:  Proc Natl Acad Sci U S A       Date:  1994-12-20       Impact factor: 11.205

8.  Restriction in the conformational flexibility of apoproteins in the presence of organic cosolvents: a consequence of the formation of "native-like conformation".

Authors:  A S Acharya; K S Iyer; G Sahni; K M Khandke; B N Manjula
Journal:  J Protein Chem       Date:  1992-10

9.  Conformational studies of alpha-globin in 1-propanol: propensity of the alcohol to limit the sites of proteolytic cleavage.

Authors:  K S Iyer; A S Acharya
Journal:  Proc Natl Acad Sci U S A       Date:  1987-10       Impact factor: 11.205

10.  High-efficiency transpeptidation catalysed by clostripain and electrostatic effects in substrate specificity.

Authors:  S Yagisawa; S Watanabe; T Takaoka; H Azuma
Journal:  Biochem J       Date:  1990-03-15       Impact factor: 3.857

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