Methods in Modern Biophysics, 2/e
暫譯: 現代生物物理學方法，第二版

Bengt Nölting

Methods in Modern Biophysics, 2/e
  • 出版商: Springer
  • 出版日期: 2005-09-06
  • 售價: $1,050
  • 貴賓價: 9.8 折 $1,029
  • 語言: 英文
  • 頁數: 257
  • 裝訂: Paperback
  • ISBN: 354027703X
  • ISBN-13: 9783540277033
  • 相關分類: 物理學 Physics

    • 下單後立即進貨 (約5~7天)

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Incorporating dramatic recent advances, "Methods in Modern Biophysics" presents a fresh and timely introduction to modern biophysical methods. This innovative text surveys and explains the ten key biophysical methods, including those related to biophysical nanotechnology, scanning probe microscopy, X-ray crystallography, ion mobility spectrometry, mass spectrometry, and proteomics. Containing much information previously unavailable in tutorial form, "Methods in Modern Biophysics" employs worked examples and more than 260 illustrations to fully detail the techniques and their underlying mechanisms. The book was written for advanced undergraduate and graduate students, postdocs, researchers, lecturers and professors in biophysics, biochemistry, general biology and related fields.

Table of contents


1 The three-dimensional structure of proteins ................................................. 1
1.1 Structure of the native state ................................................................. 1
1.2 Protein folding transition states ............................................................ 9
1.3 Structural determinants of the folding rate constants ......................... 12
1.4 Support of structure determination by protein folding simulations ......... 20
2 Liquid chromatography of biomolecules ................................................... 23
2.1 Ion exchange chromatography .............................................................. 23
2.2 Gel filtration chromatography .............................................................. 28
2.3 Affinity chromatography ...................................................................... 31
2.4 Counter-current chromatography and ultrafiltration ................................ 33
3 Mass spectrometry ................................................................................. 37
3.1 Principles of operation and types of spectrometers ................................. 37
3.1.1 Sector mass spectrometer ................................................................. 38
3.1.2 Quadrupole mass spectrometer ........................................................ 39
3.1.3 Ion trap mass spectrometer .............................................................. 39
3.1.4 Time-of-flight mass spectrometer .................................................... 40
3.1.5 Fourier transform mass spectrometer ............................................... 43
3.1.6 Ionization, ion transport and ion detection ...................................... 44
3.1.7 Ion fragmentation ............................................................................. 45
3.1.8 Combination with chromatographic methods .................................. 46
3.2 Biophysical applications ...................................................................... 49
4 X-ray structural analysis ....................................................................... 59
4.1 Fourier transform and X-ray crystallography........................................... 59
4.1.1 Fourier transform ............................................................................. 59
4.1.2 Protein X-ray crystallography .......................................................... 69
4.1.2.1 Overview .................................................................................. 69
4.1.2.2 Production of suitable crystals .................................................. 69
4.1.2.3 Acquisition of the diffraction pattern ........................................ 71
XII Contents
4.1.2.4 Determination of the phases: heavy atom replacement ............. 76
4.1.2.5 Calculation of the electron density and refinement .................. 83
4.1.2.6 Cryocrystallography and time-resolved crystallography........... 84
4.2 X-ray scattering .......................................................................... 85
4.2.1 Small angle X-ray scattering (SAXS) ............................................. 85
4.2.2 X-ray backscattering ............................................................. 88
5 Protein infrared spectroscopy ............................................................ 91
5.1 Spectrometers and devices ............................................................ 92
5.1.1 Scanning infrared spectrometers ................................................... 92
5.1.2 Fourier transform infrared (FTIR) spectrometers ............................ 92
5.1.3 LIDAR, optical coherence tomography, attenuated total
reflection and IR microscopes
................. 96
5.2 Applications .......................................................................... 102
6 Electron microscopy .................................................................. 107
6.1 Transmission electron microscope (TEM)...................................... 107
6.1.1 General design ..................................................................... 107
6.1.2 Resolution ........................................................................... 109
6.1.3 Electron sources ................................................................... 110
6.1.4 TEM grids ............................................................................. 112
6.1.5 Electron lenses ....................................................................... 112
6.1.6 Electron-sample interactions and electron spectroscopy ................ 115
6.1.7 Examples of biophysical applications ........................................... 117
6.2 Scanning transmission electron microscope (STEM) ............................ 118
7 Scanning probe microscopy .............................................................. 121
7.1 Atomic force microscope (AFM) .......................................................... 121
7.2 Scanning tunneling microscope (STM) ................................................. 133
7.3 Scanning nearfield optical microscope (SNOM) ................................... 135
7.3.1 Overcoming the classical limits of optics ...................................... 135
7.3.2 Design of the subwavelength aperture ........................................... 138
7.3.3 Examples of SNOM applications ................................................... 142
7.4 Scanning ion conductance microscope, scanning thermal
microscope and further scanning probe microscopes
.................... 143
8 Biophysical nanotechnology ............................................................... 147
8.1 Force measurements in single protein molecules .................................. 147
8.2 Force measurements in a single polymerase-DNA complex .................. 150
Contents XIII
8.3 Molecular recognition ........................................................................... 152
8.4 Protein nanoarrays and protein engineering .......................................... 155
8.5 Study and manipulation of protein crystal growth ................................. 158
8.6 Nanopipettes, molecular diodes, self-assembled nanotransistors,
nanoparticle-mediated transfection and further biophysical
nanotechnologies
......... 159
9 Proteomics: high throughput protein functional analysis ....................... 165
9.1 Target discovery .......................................................................... 166
9.2 Interaction proteomics ................................................................. 168
9.3 Chemical proteomics ................................................................... 172
9.4 Lab-on-a-chip technology and mass-spectrometric array scanners ....... 173
9.5 Structural proteomics ................................................................... 174
10 Ion mobility spectrometry .................................................................... 175
10.1 General design of spectrometers ......................................................... 175
10.2 Resolution and sensitivity ................................................................ 180
10.3 IMS-based “sniffers” ...................................................................... 183
10.4 Design details ................................................................................. 184
10.5 Detection of biological agents ......................................................... 193
11 Φ-Value analysis ............................................................................... 197
11.1 The method ..................................................................................... 197
11.2 High resolution of six protein folding transition states ....................... 199
12 Evolutionary computer programming ......................................................... 203
12.1 Reasons for the necessity of self-evolving computer programs .......... 203
12.2 General features of the method ........................................................... 203
12.3 Protein folding and structure simulations ........................................... 206
12.4 Evolution of nanooptical devices made from nanoparticles .............. 207
12.4.1 Materials and methods ................................................................ 207
12.4.2 Results and discussion ................................................................ 208
12.5 Further potential applications .............................................................. 210
13 Conclusions .................................................................................... 213
References ........................................................................................ 215
Index ................................................................................................ 247

商品描述(中文翻譯)

**描述**

《現代生物物理學方法》結合了最近的重大進展，提供了對現代生物物理方法的新穎且及時的介紹。這本創新的教材調查並解釋了十種關鍵的生物物理方法，包括與生物物理納米技術、掃描探針顯微鏡、X射線晶體學、離子遷移譜、質量譜和蛋白質組學相關的方法。《現代生物物理學方法》包含了許多以前以教學形式無法獲得的信息，並使用了實例和超過260幅插圖來詳細說明這些技術及其基本機制。本書是為高年級本科生、研究生、博士後研究員、研究人員、講師和生物物理學、生物化學、一般生物學及相關領域的教授所撰寫。

**目錄**

1 蛋白質的三維結構 ................................................. 1
1.1 本徵狀態的結構 ................................................................. 1
1.2 蛋白質摺疊過渡狀態 ............................................................ 9
1.3 摺疊速率常數的結構決定因素 ......................................... 12
1.4 蛋白質摺疊模擬對結構確定的支持 .......................... 20
2 生物分子的液相色譜 .................................................. 23
2.1 離子交換色譜 .............................................................. 23
2.2 凝膠過濾色譜 .............................................................. 28
2.3 親和色譜 ...................................................................... 31
2.4 逆流色譜和超濾 ......................................................... 33
3 質量譜 ................................................................................. 37
3.1 操作原理和質譜儀的類型 ......................................... 37
3.1.1 扇形質量譜儀 .......................................................... 38
3.1.2 四極質量譜儀 ........................................................ 39
3.1.3 離子捕獲質量譜儀 .................................................. 39
3.1.4 時間飛行質量譜儀 .................................................. 40
3.1.5 傅立葉變換質量譜儀 ............................................... 43
3.1.6 離子化、離子傳輸和離子檢測 ................................ 44
3.1.7 離子碎片化 ................................................................ 45
3.1.8 與色譜方法的結合 .................................................. 46
3.2 生物物理應用 ................................................................ 49
4 X射線結構分析 .................................................................. 59
4.1 傅立葉變換和X射線晶體學 ........................................ 59
4.1.1 傅立葉變換 .................................................................. 59
4.1.2 蛋白質X射線晶體學 .................................................. 69
4.1.2.1 概述 ........................................................................... 69
4.1.2.2 合適晶體的生成 .................................................. 69
4.1.2.3 獲取衍射圖樣 .................................................... 71
4.1.2.4 相位的確定：重原子替換 .................................. 76
4.1.2.5 電子密度的計算和精修 ...................................... 83
4.1.2.6 冷凍晶體學和時間解析晶體學 ......................... 84
4.2 X射線散射 ...................................................................... 85
4.2.1 小角X射線散射 (SAXS) ........................................... 85
4.2.2 X射線反向散射 ........................................................ 88
5 蛋白質紅外光譜學 .......................................................... 91
5.1 光譜儀和設備 .............................................................. 92
5.1.1 掃描紅外光譜儀 ...................................................... 92
5.1.2 傅立葉變換紅外 (FTIR) 光譜儀 ............................ 92
5.1.3 LIDAR、光學相干斷層掃描、衰減全反射和紅外顯微鏡 .......... 96
5.2 應用 .................................................................................. 102
6 電子顯微鏡 ........................................................................ 107
6.1 傳輸電子顯微鏡 (TEM) .................................................. 107
6.1.1 一般設計 .................................................................... 107
6.1.2 解析度 .......................................................................... 109
6.1.3 電子源 ........................................................................ 110
6.1.4 TEM 網格 .................................................................... 112
6.1.5 電子透鏡 .................................................................... 112
6.1.6 電子-樣品相互作用和電子光譜學 ......................... 115
6.1.7 生物物理應用的例子 ............................................... 117
6.2 掃描傳輸電子顯微鏡 (STEM) .................................... 118
7 掃描探針顯微鏡 .............................................................. 121
7.1 原子力顯微鏡 (AFM) .................................................... 121
7.2 掃描隧道顯微鏡 (STM) ................................................ 133
7.3 掃描近場光學顯微鏡 (SNOM) .................................... 135
7.3.1 克服光學的經典限制 ............................................. 135
7.3.2 子波長孔的設計 .................................................... 138
7.3.3 SNOM 應用的例子 .................................................. 142
7.4 掃描離子導電顯微鏡、掃描熱顯微鏡及其他掃描探針顯微鏡 .......... 143
8 生物物理納米技術 .......................................................... 147
8.1 單一蛋白質分子的力學測量 ...................................... 147
8.2 單一聚合酶-DNA 複合物的力學測量 ....................... 150
8.3 分子識別 ........................................................................ 152
8.4 蛋白質納米陣列和蛋白質工程 .................................... 155
8.5 蛋白質晶體生長的研究和操控 .................................. 158
8.6 奈米微管、分子二極體、自組裝奈米晶體管、奈米顆粒介導的轉染及其他生物物理奈米技術 .......... 159
9 蛋白質組學：高通量蛋白質功能分析 ......................... 165
9.1 目標發現 ........................................................................ 166
9.2 互作蛋白質組學 .......................................................... 168
9.3 化學蛋白質組學 .......................................................... 172
9.4 晶片實驗室技術和質譜陣列掃描儀 ......................... 173
9.5 結構蛋白質組學 .......................................................... 174
10 離子遷移譜 ...................................................................... 175
10.1 質譜儀的一般設計 ....................................................... 175
10.2 解析度和靈敏度 ........................................................ 180
10.3 基於IMS的“嗅探器” ................................................ 183
10.4 設計細節 ...................................................................... 184
10.5 生物劑的檢測 ............................................................ 193
11 Φ-值分析 ........................................................................ 197
11.1 方法 .............................................................................. 197
11.2 六種蛋白質摺疊過渡狀態的高解析度 ....................... 199
12 演化計算機編程 ............................................................ 203
12.1 自我演化計算機程序的必要性原因 ....................... 203
12.2 方法的一般特徵 ....................................................... 203
12.3 蛋白質摺疊和結構模擬 ............................................. 206
12.4 由奈米顆粒製成的納米光學設備的演化 ................. 207
12.4.1 材料和方法 ............................................................ 207
12.4.2 結果和討論 ............................................................ 208
12.5 進一步的潛在應用 .................................................... 210
13 結論 .................................................................................. 213
參考文獻 ................................................................................ 215
索引 ........................................................................................ 247

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