Studies and application of ß-hairpin stabilized by novel reverse turn composed of aminoxy acid and ß-amino acid

2015 ◽  
Author(s):  
Chun-kit Lam
Keyword(s):  
Amino Acid ◽  
Reverse Turn

An Unusual Reverse Turn Structure Adopted by a Furanoid Sugar Amino Acid Incorporated in Gramicidin S

2004 ◽  
Vol 126 (11) ◽  
pp. 3444-3446 ◽  
Author(s):  
Gijsbert M. Grotenbreg ◽  
Mattie S. M. Timmer ◽  
Antonio L. Llamas-Saiz ◽  
Martijn Verdoes ◽  
Gijsbert A. van der Marel ◽  
...  
Keyword(s):  
Amino Acid ◽  
Gramicidin S ◽  
Reverse Turn ◽  
Turn Structure

Pro-D-NMe-Amino Acid and D-Pro-NMe-Amino Acid: Simple, Efficient Reverse-Turn Constraints

1995 ◽  
Vol 117 (22) ◽  
pp. 5927-5937 ◽  
Author(s):  
David K. Chalmers ◽  
Garland R. Marshall
Keyword(s):  
Amino Acid ◽  
Reverse Turn

ChemInform Abstract: Synthesis of Spiroazabicycloalkane Amino Acid Scaffolds as Reverse-Turn Inducer Dipeptide Mimics.

ChemInform ◽  
2001 ◽  
Vol 32 (15) ◽  
pp. no-no
Author(s):  
Leonardo Manzoni ◽  
Matteo Colombo ◽  
Emanuela May ◽  
Carlo Scolastico
Keyword(s):  
Amino Acid ◽  
Reverse Turn

ChemInform Abstract: Synthesis of Azabicycloalkane Amino Acid Scaffolds as Reverse-Turn Inducer Dipeptide Mimics.

ChemInform ◽  
2001 ◽  
Vol 32 (3) ◽  
pp. no-no
Author(s):  
Mauro Angiolini ◽  
Silvia Araneo ◽  
Laura Belvisi ◽  
Edoardo Cesarotti ◽  
Anna Checchia ◽  
...  
Keyword(s):  
Amino Acid ◽  
Reverse Turn

scholarly journals Protein stabilization by tuning the steric restraint at the reverse turn

2018 ◽  
Vol 9 (20) ◽  
pp. 4600-4609 ◽  
Author(s):  
Priyanka Lahiri ◽  
Hitesh Verma ◽  
Ashraya Ravikumar ◽  
Jayanta Chatterjee
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Thermodynamic Stability ◽  
Protein Stabilization ◽  
Reverse Turn

The incorporation of pseudoallylic strain by N-methylation at the solvent exposed loop in proteins leads to a stark increase in their thermodynamic stability that can be tuned by altering the amino acid composition.

Investigation of recrystallization of collagen (I) employing contraction and statistical conformation properties

1980 ◽  
Vol 45 (2) ◽  
pp. 628-640
Author(s):  
Antonín Galatík ◽  
Anton Blažej
Keyword(s):  
Amino Acid ◽  
High Probability ◽  
Thermal Denaturation ◽  
Amino Acid Sequences ◽  
Collagen I ◽  
Helical Conformation ◽  
Conformation Analysis ◽  
Reverse Turn ◽  
Native Collagen ◽  
Collagen Chain

The ability of collagen (I) to recrystallize by cooling after a thermal denaturation was attempted by a method of concentration energy and theoretical statistical conformation analysis. Contraction energy of the native collagen was 1.96 ± 0.6 J/g; that of denaturated collagen after cooling in contracted state 0.036 J/g and in the stretched state 0.45 ± 0.1 J/g. This corresponds to a 1.8 and 22.8% of recrystallization, respectively. Theoretic calculation of the probable conformation of the whole sequence of α1(I) chain showed that approximately only 60% of sequences have the ability to form spontaneously stretched polypyrrolidine conformation, whereas approximately 34% of the chain was randomized. About 5% of amino acid sequences had a preferred α-helical conformation and terminal peptides, especially the C-tail have a high probability of extended conformation of a β-pleated sheat type. The collagen chain reveals a significant tendency to form reverse turn. Statistical conformation properties are compared with those of some model polypeptides.

ChemInform Abstract: Conformational Analysis of Azabicycloalkane Amino Acid Scaffold as Reverse-Turn Inducer Dipeptide Mimics.

ChemInform ◽  
2001 ◽  
Vol 32 (3) ◽  
pp. no-no
Author(s):  
Laura Belvisi ◽  
Anna Bernardi ◽  
Leonardo Manzoni ◽  
Donatella Potenza ◽  
Carlo Scolastico
Keyword(s):  
Amino Acid ◽  
Conformational Analysis ◽  
Reverse Turn
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