Alpha helix capping in synthetic model peptides by reciprocal side chain-main chain interactions: Evidence for an N terminal “capping box”

1994 ◽  
Vol 18 (1) ◽  
pp. 1-7 ◽  
Author(s):  
Hongxing X. Zhou ◽  
Pingchiang Lyu ◽  
David E. Wemmer ◽  
Neville R. Kallenbach
Keyword(s):  
Main Chain ◽  
Alpha Helix ◽  
Side Chain ◽  
Synthetic Model ◽  
Helix Capping ◽  
Capping Box ◽  
Model Peptides

Unifying the microscopic picture of His-containing turns: from gas phase model peptides to crystallized proteins

2017 ◽  
Vol 19 (26) ◽  
pp. 17128-17142 ◽  
Author(s):  
Woon Yong Sohn ◽  
Sana Habka ◽  
Eric Gloaguen ◽  
Michel Mons
Keyword(s):  
Gas Phase ◽  
Main Chain ◽  
Protein Structures ◽  
Phase Model ◽  
Side Chain ◽  
Central Position ◽  
Microscopic Picture ◽  
Model Peptides

The presence in crystallized proteins of a local anchoring between the side chain of a His residue, located in the central position of a γ- or β-turn, and its local main chain environment, is assessed by the comparison of protein structures with relevant isolated model peptides.

scholarly journals Alpha Helix Nucleation by a Simple Cyclic Tetrapeptide

2017 ◽  
Vol 70 (2) ◽  
pp. 213 ◽  
Author(s):  
Huy N. Hoang ◽  
Chongyang Wu ◽  
Renee L. Beyer ◽  
Timothy A. Hill ◽  
David P. Fairlie
Keyword(s):  
Alpha Helix ◽  
Biologically Relevant ◽  
Helical Peptide ◽  
Helix Nucleation ◽  
Helix Capping ◽  
N Terminus ◽  
Turn Structure ◽  
Cyclic Tetrapeptide ◽  
Model Peptides

The simple cyclic tetrapeptide cyclo-(1,4)-[Ala-Arg-Ala-homoGlu]-NH2 (3) is shown to adopt an unusual α-turn structure, which is not α-helical but can nucleate α-helicity when attached to the N-terminus of either model peptides or two biologically relevant peptides. This new N-terminal helix-capping macrocycle provides very simple and rapid synthetic access to α-helical peptide structures.

scholarly journals Charged histidine affects alpha-helix stability at all positions in the helix by interacting with the backbone charges

1993 ◽  
Vol 90 (23) ◽  
pp. 11337-11340 ◽  
Author(s):  
K M Armstrong ◽  
R L Baldwin
Keyword(s):  
Hydrogen Bonding ◽  
Central Region ◽  
Main Chain ◽  
Alpha Helix ◽  
Dipole Interaction ◽  
Major Effect ◽  
Side Chain ◽  
Histidine Residue ◽  
Helix Stability

To determine whether a charged histidine side chain affects alpha-helix stability only when histidine is close to one end of the helix or also when it is in the central region, we substitute a single histidine residue at many positions in two reference peptides and measure helix stability and histidine pKa. The position of a charged histidine residue has a major effect on helix stability in 0.01 M NaCl: the helix content of a 17-residue peptide is 24% when histidine is at position 3 compared to 76% when it is at position 17. This dependence of helix content on histidine position decreases sharply in 1 M NaCl, as expected for counterion screening of the charge-helix dipole interaction. Results at interior positions indicate that the position of a charged histidine residue affects helix stability at these positions. Unexpectedly high values of the helix content are found when either neutral or charged histidine is at one of the last three C-terminal positions, suggesting that either form can stabilize an isolated helix by hydrogen bonding to a main-chain CO group.

scholarly journals Substrate Scope for Human Histone Lysine Acetyltransferase KAT8

2021 ◽  
Vol 22 (2) ◽  
pp. 846
Author(s):  
Giordano Proietti ◽  
Yali Wang ◽  
Chiara Punzo ◽  
Jasmin Mecinović
Keyword(s):  
Main Chain ◽  
Coenzyme A ◽  
Side Chain ◽  
Histone H4 ◽  
Chemical Probes ◽  
Acetyl Coenzyme A ◽  
Acetyl Coenzyme ◽  
Histone Lysine ◽  
Lysine Acetyltransferase

Biomedically important histone lysine acetyltransferase KAT8 catalyses the acetyl coenzyme A-dependent acetylation of lysine on histone and other proteins. Here, we explore the ability of human KAT8 to catalyse the acetylation of histone H4 peptides possessing lysine and its analogues at position 16 (H4K16). Our synthetic and enzymatic studies on chemically and structurally diverse lysine mimics demonstrate that KAT8 also has a capacity to acetylate selected lysine analogues that possess subtle changes on the side chain and main chain. Overall, this work highlights that KAT8 has a broader substrate scope beyond natural lysine, and contributes to the design of new chemical probes targeting KAT8 and other members of the histone lysine acetyltransferase (KAT) family.

scholarly journals Side-Chain to Main-Chain Hydrogen Bonding Controls the Intrinsic Backbone Dynamics of the Amyloid Precursor Protein Transmembrane Helix

2014 ◽  
Vol 106 (6) ◽  
pp. 1318-1326 ◽  
Author(s):  
Christina Scharnagl ◽  
Oxana Pester ◽  
Philipp Hornburg ◽  
Daniel Hornburg ◽  
Alexander Götz ◽  
...  
Keyword(s):  
Hydrogen Bonding ◽  
Amyloid Precursor Protein ◽  
Main Chain ◽  
Transmembrane Helix ◽  
Precursor Protein ◽  
Backbone Dynamics ◽  
Side Chain
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