大学课程英汉对照分子生物学导论教学Chapter 1课件

dialyse dialysis
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ATP synthetase / ATP合成酶
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Allosteric regulation / 别构调节
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lac repressor / lac阻遏蛋白
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1.5 Experiments / 1.5 实验研究
Primary structure Secondary structure Tertiary structure Quaternary structure
生命几乎就是蛋白质 的杰作。蛋白质让生 物可以生长和繁殖。 它们为生物提供了外 形和力量，以及运动 功能。 在细胞中，蛋白质无 处不在，行使着几乎 任何功能。
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1.1 Protein Composition / 蛋白质的组成
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The twenty amino acids and their abbreviation
功能：几个例子
1.4 The Dynamics of Proteins 1.4 蛋白质动力学
1.5 Experiments
1.5 实验研究
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Chapter 1 Amino Acids to Proteins
第1章 氨基酸到蛋白质
Life is most directly the work of proteins. Proteins allow organisms to grow and reproduce. They provide shape, strength and movement. In the cell, proteins are everywhere and do almost everything.
?
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Nonpolar molecules are forced together
Water molecules get contacts with each other.
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Hydrophobic interaction / 疏水相互作用
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1.3 Protein Structure and Function
Structure adaptive to function carbonic anhydrase
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Kinesin / 驱动蛋白
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1.4 The Dynamics of Proteins
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Induced-fit vs. lock-and-key models
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Tertiary structure / 三级结构
αhelix βsheet Turn
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Quaternary structure / 四级结构
One subunit
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1.2.2 Chemical and Physical Basis for Protein Folding
Glutamine 谷氨酰胺 Gln Q
Cysteine
半胱氨酸 Cys C
Tyrosine
酪氨酸
Tyr Y
3 Basic R groups 碱性的R基团
Arginine
精氨酸
Arg R
Histidine
组氨酸
His H
Lysine
赖氨酸
Lys K
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Structures of hydrophobic amino acids
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1) Covalent bond / 共价键
H +1
+1 H
H－H
+1
+1
Covalent bond
Shared electrons
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Covalent bond / 共价键
F
W W
M
EA
IKAGSR
FPVL
Q
CIH
E
I Y
T
N
D
KG
Covalent bond
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3) Ionic bond / 离子键
Na
Cl
+11
+17
The ionic bond of sodium chloride, NaCl
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Partial charges vs. Full charges
Na
Cl
δ–
Na
Cl
+11
+17
δ+
δ+
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Ionic bond / 离子键
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Structures of the hydrophilic amino acids
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Structures of the 20 common amino acids
Negative charge
Positive charge
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The formation of a peptide bond
Physical interactions involved in protein folding 1) Covalent bonding 2) Hydrogen bonding 3) Ionic bonding 4) Van der Waals forces 5) Hydrophobic interaction
COO━ + H3N C H
CH2
CH2
C
O
O━
Glu
COO━ + H3N C H
CH2 CH2 CH2 CH2 N+ H3
Lys
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4) Van der Waals forces / 范德华力
Atom 1
Atom 2
van der Waals force
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5) Hydrophobic interaction
Chapter 1 Amino Acids to Proteins
1.1 Protein Composition
1.1 蛋白质的组成
1.2 Protein Conformations
1.2 蛋白质的构象
1.3 Protein Structure and
1.3 蛋白质的结构与
Function: A Few Examples
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1.2.1 Describing Protein Structure
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α helix / α螺旋
H N
R2 CH C
O
H N
R5 CH C
O
Hydrogen bond
(a)
(b)
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β sheet / β折叠
Hydrogen bond
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Parallel and antiparallel β sheets
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Partial double bond / 部分双键
Partial double bond
O
C N
H
OC
N+ H
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Rigid and flexible bonds
3D structure
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N-terminus and C-terminus / N-末端和C-末端
Covalent bond / 共价键
Covalent bond
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2) Hydrogen bond / 氢键
δ+H
H δ+
Oδ
δ+H
H δ+
Oδ
δ+ H
Hydrogen bond
H δ+ Oδ
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Hydrogen bond / 氢键
Hydrogen bond
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9 Hydrophobic R groups 疏水的R基团
Glycine
甘氨酸
Alanine
丙氨酸
Isoleucine 异亮氨酸
Leucine
亮氨酸
Methionine 甲硫氨酸
源自文库
Phenylalanine 苯丙氨酸
Tryptophan 色氨酸
Proline
脯氨酸
Valine
缬氨酸
Gly G Ala A Ile I Leu L Met M Phe F Trp W Pro P Val V
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1.2 Protein Conformations / 1.2 蛋白质的构象
1.2.1 Describing Protein Structure
1.2.1 描述蛋白质 的结构
1.2.2 Chemical and Physical Basis for Protein Folding
1.2.2 蛋白质折叠的 化学和物理基础
2 Acidic R groups 酸性的R基团
Aspartic acid 天冬氨酸 Asp D
Glutamic acid 谷氨酸
Glu E
6 Hydrophilic R groups 亲水的R基团
Serine
丝氨酸
Ser S
Threonine 苏氨酸
Thr T
Asparagine 天冬酰胺 Asn N