310-Helix adjoining α-helix and β-strand: Sequence and structural features and their conservation

Biopolymers ◽  
2005 ◽  
Vol 78 (3) ◽  
pp. 147-162 ◽  
Author(s):  
Lipika Pal ◽  
Bhaskar Dasgupta ◽  
Pinak Chakrabarti
Keyword(s):  
Structural Features ◽  
Α Helix ◽  
310 Helix

scholarly journals Controlling 310-Helix and α-Helix of Short Peptides in the Solid State

2007 ◽  
Vol 55 (5) ◽  
pp. 840-842 ◽  
Author(s):  
Yosuke Demizu ◽  
Masakazu Tanaka ◽  
Masanobu Nagano ◽  
Masaaki Kurihara ◽  
Mitsunobu Doi ◽  
...  
Keyword(s):  
Solid State ◽  
Short Peptides ◽  
Α Helix ◽  
310 Helix

scholarly journals Slowtert-butyl ester acidolysis and peptide 310-helix to α-helix transition in HFIP solution

Biopolymers ◽  
2007 ◽  
Vol 88 (2) ◽  
pp. 233-238 ◽  
Author(s):  
Alessandro Moretto ◽  
Marco Crisma ◽  
Fernando Formaggio ◽  
Bernard Kaptein ◽  
Quirinus B. Broxterman ◽  
...  
Keyword(s):  
Butyl Ester ◽  
Α Helix ◽  
310 Helix

Direct UV Raman Monitoring of 310-Helix and π-Bulge Premelting during α-Helix Unfolding

2006 ◽  
Vol 128 (42) ◽  
pp. 13789-13795 ◽  
Author(s):  
Aleksandr V. Mikhonin ◽  
Sanford A. Asher
Keyword(s):  
Uv Raman ◽  
Α Helix ◽  
310 Helix

Critical Main-Chain Length for Conformational Conversion From 310-Helix to α-Helix in Polypeptides

1990 ◽  
Vol 7 (6) ◽  
pp. 1321-1331 ◽  
Author(s):  
Vincenzo Pavone ◽  
Ettore Benedetti ◽  
Benedetto Di Biasio ◽  
Carlo Pedone ◽  
Antonello Santini ◽  
...  
Keyword(s):  
Chain Length ◽  
Main Chain ◽  
Α Helix ◽  
Conformational Conversion ◽  
310 Helix

scholarly journals Addition of side-chain interactions to 310-helix/coil and α-helix/310-helix/coil theory

1998 ◽  
Vol 7 (11) ◽  
pp. 2374-2383 ◽  
Author(s):  
Jia Ke Sun ◽  
Andrew J. Doig
Keyword(s):  
Side Chain ◽  
Α Helix ◽  
310 Helix

Glycogen phosphorylase revisited: extending the resolution of the R- and T-state structures of the free enzyme and in complex with allosteric activators

2021 ◽  
Vol 77 (9) ◽  
pp. 303-311
Author(s):  
Demetres D. Leonidas ◽  
Spyros E. Zographos ◽  
Katerina E. Tsitsanou ◽  
Vassiliki T. Skamnaki ◽  
George Stravodimos ◽  
...  
Keyword(s):  
Drug Design ◽  
Binding Site ◽  
Crystal Structures ◽  
Glycogen Phosphorylase ◽  
Structural Features ◽  
Terminal Segment ◽  
Structure Based Drug Design ◽  
Allosteric Transition ◽  
Α Helix ◽  
T State

The crystal structures of free T-state and R-state glycogen phosphorylase (GP) and of R-state GP in complex with the allosteric activators IMP and AMP are reported at improved resolution. GP is a validated pharmaceutical target for the development of antihyperglycaemic agents, and the reported structures may have a significant impact on structure-based drug-design efforts. Comparisons with previously reported structures at lower resolution reveal the detailed conformation of important structural features in the allosteric transition of GP from the T-state to the R-state. The conformation of the N-terminal segment (residues 7–17), the position of which was not located in previous T-state structures, was revealed to form an α-helix (now termed α0). The conformation of this segment (which contains Ser14, phosphorylation of which leads to the activation of GP) is significantly different between the T-state and the R-state, pointing in opposite directions. In the T-state it is packed between helices α4 and α16 (residues 104–115 and 497–508, respectively), while in the R-state it is packed against helix α1 (residues 22′–38′) and towards the loop connecting helices α4′ and α5′ of the neighbouring subunit. The allosteric binding site where AMP and IMP bind is formed by the ordering of a loop (residues 313–326) which is disordered in the free structure, and adopts a conformation dictated mainly by the type of nucleotide that binds at this site.

First Homo-Peptides Undergoing a Reversible 310-Helix to α-Helix ransition

2009 ◽  
pp. 49-50
Author(s):  
Alessandro Moretto ◽  
Marco Crisma ◽  
Fernando Formaggio ◽  
Claudio Toniolo ◽  
Ling Wu ◽  
...  
Keyword(s):  
Α Helix ◽  
310 Helix

Estimating the relative populations of 310-helix and α-helix in Ala-rich peptides: a hydrogen exchange and high field NMR study

1997 ◽  
Vol 267 (4) ◽  
pp. 963-974 ◽  
Author(s):  
Glenn L Millhauser ◽  
Chris J Stenland ◽  
Paul Hanson ◽  
Kimberly A Bolin ◽  
Frank J.M van de Ven
Keyword(s):  
High Field ◽  
Hydrogen Exchange ◽  
Nmr Study ◽  
Α Helix ◽  
310 Helix

Behaviour of Human Blood Serum Orosomucoid (Acid α1-Glycoprotein) in the Presence of Small Aliphatic Alcohols

1993 ◽  
Vol 58 (11) ◽  
pp. 2701-2714 ◽  
Author(s):  
Vladimír Karpenko ◽  
Ludmila Šinkorová ◽  
Ludmila Janáčková
Keyword(s):  
Volume Fraction ◽  
Structural Features ◽  
Uv Spectra ◽  
Optical Methods ◽  
Mathematical Basis ◽  
Helix Formation ◽  
Spectral Peaks ◽  
Electrostatic Contribution ◽  
The Stability ◽  
Α Helix

The influence of both methanol and ethanol on the stability of orosomucoid molecule was studied over a broad range of alcohol concentrations (volume fraction 0 - 70%) and pH between 7 and 12. The data obtained by optical methods were compared with information from prediction studies which were focused on the structural features and physicochemical parameters of amino acid in the orosomucoid molecule. From this analysis the following conclusions can be drawn: (i) ethanol exerts a more pronounced effect on α-helix formation than methanol does, (ii) at higher pH the electrostatic contribution is the crucial effect in the destabilization of the orosomucoid molecule, (iii) out of 12 phenylalanines in the orosomucoid molecule only 1 - 2 are exposed to the solvent; of the residues which are not subjected to substitution appears to be Phe 141, (iv) its neighbor, Tyr 142, appears to be a key residue, the dissociation of which destabilizes one of two longer helical segments of the orosomucoid molecule, (v) the limits of applicability of the four-derivatives of UV spectra with respect to phenylalanines were examined; analysis of the data is recommended on a more precise mathematical basis, taking into consideration the bandwidth of the spectral peaks.

scholarly journals Conformational change in elastase following complexation with alpha1-proteinase inhibitor: a CD investigation

2003 ◽  
Vol 370 (1) ◽  
pp. 345-349 ◽  
Author(s):  
Jean-Alain BOUSQUET ◽  
Jérôme DURANTON ◽  
Yves MÉLY ◽  
Joseph G. BIETH
Keyword(s):  
Proteinase Inhibitor ◽  
Tertiary Structure ◽  
Structural Features ◽  
Single Step ◽  
Thermal Unfolding ◽  
Elastase Inhibitor ◽  
Cd Spectrum ◽  
Pi Complex ◽  
Step Transition ◽  
Α Helix

The CD spectrum of porcine pancreatic elastase in complex with α1-proteinase inhibitor (α1-PI) was calculated by subtracting the CD spectrum of the proteolytically cleaved inhibitor from that of the elastase—α1-PI complex. Elastase undergoes a moderate secondary structure change: its β-structure is partially disordered while its α-helix content is poorly affected. In contrast, its tertiary structure undergoes a significant structural loosening upon complexation. These alterations have been compared with those following chemical and thermal unfolding of free elastase. Inhibitor-bound elastase and the denaturation intermediate of free elastase share secondary but not tertiary structural features. On the other hand, both free and complexed elastases undergo a single-step transition in tertiary structure upon thermal unfolding. These data are discussed in terms of the inhibition and structural modification of elastase induced by α1-PI observed by previous investigators.

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