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

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.

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On the turn-inducing properties of asparagine: the structuring role of the amide side chain, from isolated model peptides to crystallized proteins

Physical Chemistry Chemical Physics ◽

10.1039/c7cp07605c ◽

2018 ◽

Vol 20 (5) ◽

pp. 3411-3423 ◽

Cited By ~ 6

Author(s):

S. Habka ◽

W. Y. Sohn ◽

V. Vaquero-Vara ◽

M. Géléoc ◽

B. Tardivel ◽

...

Keyword(s):

Gas Phase ◽

Laser Spectroscopy ◽

Protein Structures ◽

Side Chain ◽

Amide Side Chain ◽

Model Peptides

The anchoring properties of an asparagine (Asn) residue to its local backbone environment in turn model peptides is characterized using gas phase laser spectroscopy and compared to crystallized protein structures.

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

Proteins Structure Function and Bioinformatics ◽

10.1002/prot.340180103 ◽

1994 ◽

Vol 18 (1) ◽

pp. 1-7 ◽

Cited By ~ 72

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

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Deterministic features of side-chain main-chain hydrogen bonds in globular protein structures

Protein Engineering Design and Selection ◽

10.1093/protein/13.4.227 ◽

2000 ◽

Vol 13 (4) ◽

pp. 227-238 ◽

Cited By ~ 67

Author(s):

Narayanan Eswar ◽

C. Ramakrishnan

Keyword(s):

Hydrogen Bonds ◽

Main Chain ◽

Protein Structures ◽

Globular Protein ◽

Side Chain

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On the correlation between the main-chain and side-chain atomic displacement parameters (Bvalues) in high-resolution protein structures

Acta Crystallographica Section D Biological Crystallography ◽

10.1107/s0907444998006611 ◽

1999 ◽

Vol 55 (1) ◽

pp. 173-180 ◽

Cited By ~ 7

Author(s):

S. Parthasarathy ◽

M. R. N. Murthy

Keyword(s):

High Resolution ◽

Main Chain ◽

Protein Structures ◽

Atomic Displacement ◽

Side Chain ◽

Atomic Displacement Parameters

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Faculty Opinions recommendation of Main chain and side chain dynamics of oxidized flavodoxin from Cyanobacterium anabaena.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.1002693.29208 ◽

2001 ◽

Author(s):

Vincent Rotello

Keyword(s):

Main Chain ◽

Side Chain ◽

Chain Dynamics ◽

Cyanobacterium Anabaena ◽

Side Chain Dynamics

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Electron-Transfer-Induced Side-Chain Cleavage in Tryptophan Facilitated through Potassium-Induced Transition-State Stabilization in the Gas Phase

The Journal of Physical Chemistry A ◽

10.1021/acs.jpca.1c00690 ◽

2021 ◽

Author(s):

Filipe Ferreira da Silva ◽

Tiago Cunha ◽

Andre Rebelo ◽

Adrià Gil ◽

Maria José Calhorda ◽

...

Keyword(s):

Electron Transfer ◽

Transition State ◽

Gas Phase ◽

Side Chain ◽

Side Chain Cleavage ◽

Transition State Stabilization ◽

Chain Cleavage

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Substrate Scope for Human Histone Lysine Acetyltransferase KAT8

International Journal of Molecular Sciences ◽

10.3390/ijms22020846 ◽

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.

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