On the Role of Aromatic Side Chains in the Photoactivation of BLUF Domains†

Biochemistry ◽  
2007 ◽  
Vol 46 (25) ◽  
pp. 7405-7415 ◽  
Author(s):  
Magdalena Gauden ◽  
Jeffrey S. Grinstead ◽  
Wouter Laan ◽  
Ivo H. M. van Stokkum ◽  
Marcela Avila-Perez ◽  
...  
Keyword(s):  
Side Chains ◽  
Aromatic Side Chains

scholarly journals Free Energy Landscape and Rate Estimation of the Aromatic Ring Flips in Basic Pancreatic Trypsin Inhibitor Using Metadynamics

2021 ◽  
Author(s):  
Pär Söderhjelm ◽  
Mandar Kulkarni
Keyword(s):  
Free Energy ◽  
Trypsin Inhibitor ◽  
Side Chain ◽  
Side Chains ◽  
Aromatic Residues ◽  
Basic Pancreatic Trypsin Inhibitor ◽  
Pancreatic Trypsin Inhibitor ◽  
Energy Surfaces ◽  
Aromatic Side Chains

Aromatic side-chains (phenylalanine and tyrosine) of a protein flip by 180° around the Cβ-Cγ axis (χ2 dihedral of side-chain) producing two symmetry-equivalent states. The ring-flip dynamics act as an NMR probe to understand local conformational fluctuations. Ring-flips are categorized as slow (ms onwards) or fast (ns to near ms) based on timescales accessible to NMR experiments. In this study, we investigated the ability of the infrequent metadynamics approach to discriminate between slow and fast ring-flips for eight individual aromatic side-chains (F4, Y10, Y21, F22, Y23, F33, Y35, F45) of basic pancreatic trypsin inhibitor (BPTI). Well-tempered metadynamics simulations were performed to observe ring-flipping free energy surfaces for all eight aromatic residues. The results indicate that χ2 as a standalone collective variable (CV) is not sufficient to classify fast and slow ring-flips. Most of the residues needed χ1 (N−Cχα) as a complementary CV, indicating the importance of librational motions in ring-flips. Multiple pathways and mechanisms were observed for residues F4, Y10, and F22. Recrossing events are observed for residues F22 and F33, indicating a possible role of friction effects in the ring-flipping. The results demonstrate the successful application of the metadynamics based approach to estimate ring-flip rates of aromatic residues in BPTI and identify certain limitations of the approach.

scholarly journals Role of Aromatic Side Chains in Amyloid β-Protein Aggregation

2012 ◽  
Vol 3 (12) ◽  
pp. 1008-1016 ◽  
Author(s):  
Risto Cukalevski ◽  
Barry Boland ◽  
Birgitta Frohm ◽  
Eva Thulin ◽  
Dominic Walsh ◽  
...  
Keyword(s):  
Protein Aggregation ◽  
Amyloid Β ◽  
Side Chains ◽  
Amyloid Β Protein ◽  
Β Protein ◽  
Aromatic Side Chains

Role of Aromatic Side Chains in the Folding and Thermodynamic Stability of Integral Membrane Proteins

2007 ◽  
Vol 129 (26) ◽  
pp. 8320-8327 ◽  
Author(s):  
Heedeok Hong ◽  
Sangho Park ◽  
Ricardo H. Flores Jiménez ◽  
Dennis Rinehart ◽  
Lukas K. Tamm
Keyword(s):  
Membrane Proteins ◽  
Thermodynamic Stability ◽  
Integral Membrane Proteins ◽  
Side Chains ◽  
Aromatic Side Chains

The role of aromatic side chains on the supramolecular hydrogelation of naphthalimide/dipeptide conjugates

2018 ◽  
Vol 42 (6) ◽  
pp. 4443-4449 ◽  
Author(s):  
Shu-Min Hsu ◽  
Rajan Deepan Chakravarthy ◽  
Hsun Cheng ◽  
Fang-Yi Wu ◽  
Tsung-Sheng Lai ◽  
...  
Keyword(s):  
Amino Acid ◽  
Side Chain ◽  
Side Chains ◽  
Amino Acid Side Chain ◽  
Aromatic Side Chains

This study demonstrates the influence of an amino-acid side chain of NI-dipeptides on supramolecular hydrogelation and biocompatibility.

The role of aromatic side-chains in amyloid growth and membrane interaction of the islet amyloid polypeptide fragment LANFLVH

2010 ◽  
Vol 40 (1) ◽  
pp. 1-12 ◽  
Author(s):  
Danilo Milardi ◽  
Michele F. M. Sciacca ◽  
Matteo Pappalardo ◽  
Domenico M. Grasso ◽  
Carmelo La Rosa
Keyword(s):  
Islet Amyloid Polypeptide ◽  
Side Chains ◽  
Islet Amyloid ◽  
Membrane Interaction ◽  
Aromatic Side Chains

Privileged hydration sites in aromatic side chains: effect on conformational equilibrium

2017 ◽  
Vol 19 (42) ◽  
pp. 28684-28695 ◽  
Author(s):  
Belén Hernández ◽  
Fernando Pflüger ◽  
Manuel Dauchez ◽  
Mahmoud Ghomi
Keyword(s):  
Conformational Equilibrium ◽  
Theoretical Calculations ◽  
Side Chains ◽  
Aromatic Side Chains

The most energetically favourable hydration sites of aromatic (Phe, Tyr, Trp and His) side chains revealed by DFT-based theoretical calculations.

Heparan sulfate side chains have a critical role in the inhibitory effects of perlecan on vascular smooth muscle cell response to arterial injury

2014 ◽  
Vol 307 (3) ◽  
pp. H337-H345 ◽  
Author(s):  
Lara Gotha ◽  
Sang Yup Lim ◽  
Azriel B. Osherov ◽  
Rafael Wolff ◽  
Beiping Qiang ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Critical Role ◽  
Arterial Injury ◽  
Side Chains ◽  
Wild Type ◽  
Injury Response ◽  
Migratory Response

Perlecan is a proteoglycan composed of a 470-kDa core protein linked to three heparan sulfate (HS) glycosaminoglycan chains. The intact proteoglycan inhibits the smooth muscle cell (SMC) response to vascular injury. Hspg2Δ3/Δ3 (MΔ3/Δ3) mice produce a mutant perlecan lacking the HS side chains. The objective of this study was to determine differences between these two types of perlecan in modifying SMC activities to the arterial injury response, in order to define the specific role of the HS side chains. In vitro proliferative and migratory activities were compared in SMC isolated from MΔ3/Δ3 and wild-type mice. Proliferation of MΔ3/Δ3 SMC was 1.5× greater than in wild type ( P < 0.001), increased by addition of growth factors, and showed a 42% greater migratory response than wild-type cells to PDGF-BB ( P < 0.001). In MΔ3/Δ3 SMC adhesion to fibronectin, and collagen types I and IV was significantly greater than wild type. Addition of DRL-12582, an inducer of perlecan expression, decreased proliferation and migratory response to PDGF-BB stimulation in wild-type SMC compared with MΔ3/Δ3. In an in vivo carotid artery wire injury model, the medial thickness, medial area/lumen ratio, and macrophage infiltration were significantly increased in the MΔ3/Δ3 mice, indicating a prominent role of the HS side chain in limiting vascular injury response. Mutant perlecan that lacks HS side chains had a marked reduction in the inhibition of in vitro SMC function and the in vivo arterial response to injury, indicating the critical role of HS side chains in perlecan function in the vessel wall.

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