Dissertation > Excellent graduate degree dissertation topics show

Generalized Two-dimensional Correlation Spectroscopic Studies on the Structural Changes of Proteins Induced by Environmental Variations

Author: XieZuo
Tutor: HuangHe
School: Wuhan University of Technology
Course: Materials Science
Keywords: Protein Secondary Structure Generalized two-dimensional correlation spectroscopy Curve fitting Adsorption Fluorescence Quenching
CLC: R284
Type: Master's thesis
Year: 2011
Downloads: 37
Quote: 0
Read: Download Dissertation

Abstract

Generalized two-dimensional correlation spectroscopy technology has been widely applied to the solution of environmental perturbations induced changes in protein secondary structure. The one thing in common in these studies is the use of a generalized two-dimensional correlation spectroscopy basic advantage, namely the so-called \A basic problem is commonly stated in the existing research: the changes in the protein structure is not a completely collaborative process, but the presence of the sequence order. Generalized two-dimensional correlation spectroscopy, however, there are still some problems. Existing studies (including our own) that one of the two basic advantages spectroscopy: spectral resolving power can be increased, there is a lot of uncertainty, the peak resolution may be because the peak shift, peak width changes and other factors led to the false peak; recent findings also show that its second big advantage: the peak intensity changes in the role of outside interference, \The subject using a generalized two-dimensional correlation spectroscopy methods combined with in situ spectral analysis of several typical environment-induced changes in the protein structure process and change mechanism research; same time, the existing problems in the generalized two-dimensional correlation spectroscopy authentication, provide the basis for further perfect the theory of generalized two-dimensional correlation spectroscopy method to learn. The specific contents are as follows: a study of human serum albumin in the adsorption process of the ATR crystal surface, dimensional correlation analysis of more than the second derivative method to distinguish the three new peak may be caused due to peak displacement. The following partial spectra obtained by in situ changes in the intensity of the three sub-peak \1. The content of the results represented by the peak area of ??human serum albumin adsorption process is divided into three stages: 25 minutes ago, no obvious change in the secondary structure of the protein; 25 minutes to 50 minutes, the α helix content reduce the conversion for a short part of the extended chain and random coil structure, three secondary structure changes occur simultaneously; 50 minutes later, the α helix content flatten small corner and stretch the chain structure slowly transform into random coil structure . 2 β-lactoglobulin secondary structure changes in the ATR crystal surface adsorption process. Situ spectra obtained 1627,1651,1684 cm-1 at the peak intensity changes prior to 1666 cm-1. 15 minutes before, the size of the three peak intensity of the rate of change: 1627 (7.38E-4) GT; 1651 (6.83E-4) GT; 1684 (3.21E-4) cm-1. Content changes by the peak area calculation result: the adsorption of the first 10 minutes, β-Lg no significant secondary structural changes; 10 minutes to 15 minutes, antiparallel β-sheet (low wavenumber part of the 1627 cm-1) decreased and to change the order of the random structure portion (1651 cm-1); p-corner (1666cm-1) of the content of the β-sheet (high wave number of portion 1684 cm-1) did not change significantly 20 minutes before the adsorbed. After 20 minutes, the content of the p-corner structure (1666 cm-1) decreased slightly and to change the order of the anti-parallel β-sheet (part 1684 cm-1) of the high wave number different quencher (sodium iodide, and acrylamide quenching process) Myoglobin two tryptophan residues (W7 and W14). The in situ fluorescence analysis: W7 and W14 of the strength of NaI and AA role both at the same time changes, there is no local sequence order. IR Studies obtained the HM solution as the concentration decreases generating portion unfolding use W14 the environment (10μM) than under hydrophobic at higher concentrations (2 mM), iodide ion can enter and quenching the fluorescence. Since and W7 is exposed to the water phase, so NaI faster the quenching the W7 of fluorescence, AA W7 and W14 quenching rate of the fluorescence intensity is substantially the same. Generalized two-dimensional correlation spectroscopy analysis of the above three systems, and found that the overall sequence order are inconsistent and in situ spectroscopic analysis of the results obtained.

Related Dissertations

CLC: > Medicine, health > Chinese Medicine > Of Pharmacy > Traditional Chinese medicine chemical
© 2012 www.DissertationTopic.Net Mobile