scholarly journals The fully‐extended conformation in peptides and proteins

2018 ◽  
Vol 110 (5) ◽  
pp. e23100 ◽  
Author(s):  
Marco Crisma ◽  
Fernando Formaggio ◽  
Carlos Alemán ◽  
Joan Torras ◽  
Chandrasekharan Ramakrishnan ◽  
...  
Keyword(s):  
Extended Conformation ◽  
Fully Extended Conformation

Characterizing the denatured state ensemble of ubiquitin under native conditions using replica exchange molecular dynamics

RSC Advances ◽  
2016 ◽  
Vol 6 (98) ◽  
pp. 95584-95589
Author(s):  
Nai-yuan Chang ◽  
Yi-Ci Li ◽  
Cheng-Ping Jheng ◽  
Yu-Ting Kuo ◽  
Cheng-I Lee
Keyword(s):  
Molecular Dynamics ◽  
Replica Exchange ◽  
Denatured State ◽  
Replica Exchange Molecular Dynamics ◽  
Extended Conformation ◽  
State Ensemble ◽  
Native Condition ◽  
Fully Extended Conformation

The representative structures of the denatured state ensemble of ubiquitin under a native condition and heat-denatured ubiquitin simulated from a fully extended conformation.

Onset of the fully extended conformation in (αMe)Leu derivatives and short peptides

1994 ◽  
Vol 16 (1) ◽  
pp. 7-14 ◽  
Author(s):  
C. Toniolo ◽  
M. Pantano ◽  
F. Formaggio ◽  
M. Crisma ◽  
G.M. Bonora ◽  
...  
Keyword(s):  
Short Peptides ◽  
Extended Conformation ◽  
Fully Extended Conformation

Novel peptide foldameric motifs: a step forward in our understanding of the fully-extended conformation/310-helix coexistence

2012 ◽  
Vol 10 (12) ◽  
pp. 2413 ◽  
Author(s):  
Fernando Formaggio ◽  
Marco Crisma ◽  
Gema Ballano ◽  
Cristina Peggion ◽  
Mariano Venanzi ◽  
...  
Keyword(s):  
Extended Conformation ◽  
Fully Extended Conformation ◽  
310 Helix

First unequivocal observation of the multiple fully extended conformation (25-helix) in a homopeptide from a Cα-methylated chiral α-amino acid

1995 ◽  
Vol 1 (4) ◽  
pp. 157-162 ◽  
Author(s):  
André Aubry ◽  
Valerio Del Duca ◽  
Monica Pantano ◽  
Fernando Formaggio ◽  
Marco Crisma ◽  
...  
Keyword(s):  
Amino Acid ◽  
Extended Conformation ◽  
Fully Extended Conformation

Synthese, Kristallstruktur und Konformation von N-Acetyl-Cα,α-diethylglycin/Synthesis and Crystal Structure of N-Acetyl-Cα,α-diethylglycine

1992 ◽  
Vol 47 (1) ◽  
pp. 90-92 ◽  
Author(s):  
Zdzisław Gałdecki ◽  
Bernard Luciak ◽  
Adam S. Redliński ◽  
Krzysztof Kaczmarek ◽  
Mirosław T. Leplawy
Keyword(s):  
Crystal Structure ◽  
Amino Acid ◽  
Free Amino Acid ◽  
Free Amino ◽  
Direct Methods ◽  
Monoclinic Space Group ◽  
Synthesis And Crystal Structure ◽  
Space Group ◽  
Extended Conformation ◽  
Fully Extended Conformation

The compound CH3-CO-NH-C(C2H5)2-COOH was synthesized from the corresponding free amino acid. N-Acetyl-Cα,α-diethylglycine crystallizes in the monoclinic space group P21/c with a = 13.551(2)Å, b = 11.110(3)Å, c = 13.569(3)Å, β = 111.54(2)°, Z = 8 , D = 1.21 g/cm3. This structure was solved by direct methods and refined to R = 0.084. N-Acetyl-Cα,α-diethylglycine shows a fully extended conformation in its -N H-C(C2H5)2-CO- part.

β-Peptoids: synthesis of a novel dimer having a fully extended conformation

Amino Acids ◽  
2012 ◽  
Vol 43 (5) ◽  
pp. 2005-2014 ◽  
Author(s):  
Gianluca Martelli ◽  
Antonella Monsignori ◽  
Mario Orena ◽  
Samuele Rinaldi ◽  
Nicola Castellucci ◽  
...  
Keyword(s):  
Extended Conformation ◽  
Fully Extended Conformation

scholarly journals (2Z)-2-Benzylidene-4-octadecyl-3,4-dihydro-2H-1,4-benzothiazin-3-one

IUCrData ◽  
2017 ◽  
Vol 2 (5) ◽  
Author(s):  
Nada Kheira Sebbar ◽  
Mohamed Ellouz ◽  
Sanae Lahmidi ◽  
Fouzia Hlimi ◽  
El Mokhtar Essassi ◽  
...  
Keyword(s):  
Hydrogen Bonds ◽  
Title Compound ◽  
Extended Conformation ◽  
Compound C ◽  
Thiazine Ring ◽  
Fully Extended Conformation

The octadecyl chain in the title compound, C33H47NOS, is in the `fully extended' conformation. A puckering analysis of the thiazine ring was performed. The molecules form micellar blocks in the crystal by intercalation of the extended octadecyl chains and association of the dihydro benzothiazine units through C—H...O hydrogen bonds. These blocks are associated through intercalation of the pendant phenyl groups which reside on the outer edges of each block.

scholarly journals Immunoelectron microscopic evidence for the extended conformation of light chains in clathrin trimers

1993 ◽  
Vol 268 (14) ◽  
pp. 10268-10273
Author(s):  
T. Kirchhausen ◽  
T. Toyoda
Keyword(s):  
Light Chains ◽  
Microscopic Evidence ◽  
Extended Conformation

Designing of suitable linkers for the chimeric proteins to achieve the desired flexibility and extended conformation

2018 ◽  
Vol 11 (3) ◽  
pp. 236
Author(s):  
Manoj Patidar ◽  
Naveen Yadav ◽  
Sarat K. Dalai
Keyword(s):  
Chimeric Proteins ◽  
Extended Conformation

scholarly journals Ligand-induced conformational rearrangements regulate the switch between membrane-proximal and distal functions of Rho kinase 2

2020 ◽  
Vol 3 (1) ◽  
Author(s):  
István Hajdú ◽  
András Szilágyi ◽  
Barbara M. Végh ◽  
András Wacha ◽  
Dániel Györffy ◽  
...  
Keyword(s):  
Structural Model ◽  
Coiled Coil ◽  
Rho Kinase ◽  
Mechanistic Explanation ◽  
Kinase Domain ◽  
Multifunctional Protein ◽  
Regulatory Domains ◽  
Extended Conformation ◽  
Activity Measurements ◽  
Present Solution

AbstractRho-associated protein kinase 2 (ROCK2) is a membrane-anchored, long, flexible, multidomain, multifunctional protein. Its functions can be divided into two categories: membrane-proximal and membrane-distal. A recent study concluded that membrane-distal functions require the fully extended conformation, and this conclusion was supported by electron microscopy. The present solution small-angle X-ray scattering (SAXS) study revealed that ROCK2 population is a dynamic mixture of folded and partially extended conformers. Binding of RhoA to the coiled-coil domain shifts the equilibrium towards the partially extended state. Enzyme activity measurements suggest that the binding of natural protein substrates to the kinase domain breaks up the interaction between the N-terminal kinase and C-terminal regulatory domains, but smaller substrate analogues do not. The present study reveals the dynamic behaviour of this long, dimeric molecule in solution, and our structural model provides a mechanistic explanation for a set of membrane-proximal functions while allowing for the existence of an extended conformation in the case of membrane-distal functions.

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