Exploring the impact of the side-chain length on peptide/RNA binding events

The impact of the amino-acid side-chain length on peptide–RNA binding events has been investigated using HIV-1 Tat derived peptides as ligands and the HIV-1 TAR RNA element as an RNA model.

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Effect of charged amino acid side chain length on lateral cross-strand interactions between carboxylate- and guanidinium-containing residues in a β-hairpin

Amino Acids ◽

10.1007/s00726-015-1916-2 ◽

2015 ◽

Vol 47 (5) ◽

pp. 885-898 ◽

Cited By ~ 4

Author(s):

Hsiou-Ting Kuo ◽

Shing-Lung Liu ◽

Wen-Chieh Chiu ◽

Chun-Jen Fang ◽

Hsien-Chen Chang ◽

...

Keyword(s):

Amino Acid ◽

Chain Length ◽

Side Chain ◽

Amino Acid Side Chain ◽

Side Chain Length

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Crucial Effects of Amino Acid Side Chain Length in Transmembrane Segment 5 on Substrate Affinity in Yeast Glucose Transporter Hxt7

Biochemistry ◽

10.1021/bi200958s ◽

2011 ◽

Vol 50 (40) ◽

pp. 8674-8681 ◽

Cited By ~ 17

Author(s):

Toshiko Kasahara ◽

Kosuke Shimogawara ◽

Michihiro Kasahara

Keyword(s):

Amino Acid ◽

Chain Length ◽

Glucose Transporter ◽

Side Chain ◽

Substrate Affinity ◽

Amino Acid Side Chain ◽

Transmembrane Segment ◽

Side Chain Length

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Effect of Charged Amino Acid Side Chain Length at Non-Hydrogen Bonded Strand Positions on β-Hairpin Stability

Biochemistry ◽

10.1021/bi400911p ◽

2013 ◽

Vol 52 (44) ◽

pp. 7785-7797 ◽

Cited By ~ 8

Author(s):

Li-Hung Kuo ◽

Jhe-Hao Li ◽

Hsiou-Ting Kuo ◽

Cheng-Yun Hung ◽

Hsin-Yun Tsai ◽

...

Keyword(s):

Amino Acid ◽

Chain Length ◽

Side Chain ◽

Amino Acid Side Chain ◽

Side Chain Length ◽

Hydrogen Bonded

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Effect of the basic amino-acid side chain length and the penultimate residue on the hydrolysis of benzoyldipeptides by carboxypeptidase B

Canadian Journal of Biochemistry ◽

10.1139/o78-048 ◽

1978 ◽

Vol 56 (5) ◽

pp. 315-318 ◽

Cited By ~ 4

Author(s):

Graham J. Moore ◽

N. Leo Benoiton

Keyword(s):

Amino Acid ◽

Chain Length ◽

Basic Amino Acid ◽

Side Chain ◽

Amino Acid Side Chain ◽

Carboxypeptidase B ◽

Side Chain Length ◽

C Terminus ◽

Guanidino Group ◽

Hydrolysis Of

The kinetic parameters Km and kcat/Km have been determined for the carboxypeptidase B (CPB, EC 3.4.12.3) catalyzed hydrolysis of benzoylglycyl-DL-homolysine and benzoylglycyl-L-homoarginine. Plots of these data and those for Bz-Gly-Orn and Bz-Gly-Arg (Wolff, E. C., Schirmer, E. W. &Folk, J. E. (1962) J. Biol. Chem. 237, 3094–3099) and Bz-Gly-Lys versus the length of the side chain of the basic amino acid indicate that unlike trypsin (EC 3.4.21.4) (Seely, J. H. &Benoiton, N. L. (1970) Can. J. Biochem. 48, 1122–1131) CPB has a higher binding affinity for a guanidino group than for an amino group at the side chain of the substrate C-terminus. On the other hand, CPB is similar to trypsin (ibid) in that the best substrate would have a side chain length between those of lysine and arginine.Studies with Bz-MeGly-Lys and Bz-Ala-Lys showed that the former is very slowly hydrolyzed by CPB but that the latter is a good substrate, with a high affinity for the enzyme, indicative of considerable participation of the Cα-methyl group of alanine in the binding of the substrate to the enzyme.

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Investigating peptide sequence variations for ‘double-click’ stapled p53 peptides

Organic & Biomolecular Chemistry ◽

10.1039/c4ob00742e ◽

2014 ◽

Vol 12 (24) ◽

pp. 4074-4077 ◽

Cited By ~ 38

Author(s):

Yu Heng Lau ◽

Peterson de Andrade ◽

Niklas Sköld ◽

Grahame J. McKenzie ◽

Ashok R. Venkitaraman ◽

...

Keyword(s):

Amino Acid ◽

Point Mutation ◽

Chain Length ◽

Peptide Sequence ◽

Side Chain ◽

Amino Acid Side Chain ◽

Side Chain Length ◽

Sequence Variations ◽

P53 Peptides

Evaluating the influence of staple position, azido amino acid side-chain length and point mutation on the activity of ‘double-click’ stapled p53 peptides.

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